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Vaccine Comparison

5CVMB
Vaccine Information
  • Vaccine Name: 5CVMB
  • Vaccine Ontology ID: VO_0011348
  • Type: Subunit vaccine
  • Status: Licensed
  • Antigen: Five antigens are included: GNA2132, GNA1870, NadA, GNA1030, and GNA2091 (Giuliani et al., 2006)
  • Adjuvant:
    • VO ID: VO_0000127
    • Description: Adjuvant: aluminum hydroxide combined with CpG oligonucleotides (Giuliani et al., 2006)
  • Adjuvant:
  • Immunization Route: Intraperitoneal injection (i.p.)
References
Giuliani et al., 2006: Giuliani MM, Adu-Bobie J, Comanducci M, Aricò B, Savino S, Santini L, Brunelli B, Bambini S, Biolchi A, Capecchi B, Cartocci E, Ciucchi L, Di Marcello F, Ferlicca F, Galli B, Luzzi E, Masignani V, Serruto D, Veggi D, Contorni M, Morandi M, Bartalesi A, Cinotti V, Mannucci D, Titta F, Ovidi E, Welsch JA, Granoff D, Rappuoli R, Pizza M. A universal vaccine for serogroup B meningococcus. Proceedings of the National Academy of Sciences of the United States of America. 2006; 103(29); 10834-10839. [PubMed: 16825336].
A. pleuropneumoniae ApxIa and ApxIIa protein vaccine
Vaccine Information
  • Vaccine Name: A. pleuropneumoniae ApxIa and ApxIIa protein vaccine
  • Vaccine Ontology ID: VO_0011384
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: A. pleuropneumoniae ApxIa and ApxIIa
  • apxIIA gene engineering:
    • Type: Recombinant protein preparation
    • Description: The apxIIA gene was cloned from A. pleuropneumoniae serotype 5 isolated from the lungs of Korean pigs with pleuropneumonia. For the oral vaccine, S. cerevisiae expressing ApxIA antigen as well as the ApxIIA antigen were prepared (Shin et al., 2007).
    • Detailed Gene Information: Click Here.
  • apxIA gene engineering:
    • Type: Recombinant protein preparation
    • Description: The apxIA gene was cloned from A. pleuropneumoniae serotype 5 isolated from the lungs of Korean pigs with pleuropneumonia. For the oral vaccine, S. cerevisiae expressing ApxIA antigen as well as the ApxIIA antigen were prepared (Shin et al., 2007).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Adjuvant:
  • Vector: Saccharomyces cerevisiae
  • Immunization Route: Oral immunization
References
Shin et al., 2007: Shin SJ, Shin SW, Kang ML, Lee DY, Yang MS, Jang YS, Yoo HS. Enhancement of protective immune responses by oral vaccination with Saccharomyces cerevisiae expressing recombinant Actinobacillus pleuropneumoniae ApxIA or ApxIIA in mice. Journal of veterinary science. 2007; 8(4); 383-392. [PubMed: 17993753].
A. pleuropneumoniae ApxIA protein vaccine
Vaccine Information
  • Vaccine Name: A. pleuropneumoniae ApxIA protein vaccine
  • Vaccine Ontology ID: VO_0011356
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: ApxIA (Shin et al., 2007)
  • apxIA gene engineering:
    • Type: Recombinant protein preparation
    • Description: The apxIA gene was cloned from A. pleuropneumoniae serotype 5 isolated from the lungs of Korean pigs with pleuropneumonia. For the oral vaccine, S. cerevisiae expressing ApxIA antigen were prepared (Shin et al., 2007)
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Vector: Saccharomyces cerevisiae (Shin et al., 2007)
  • Immunization Route: Oral immunization
References
Shin et al., 2007: Shin SJ, Shin SW, Kang ML, Lee DY, Yang MS, Jang YS, Yoo HS. Enhancement of protective immune responses by oral vaccination with Saccharomyces cerevisiae expressing recombinant Actinobacillus pleuropneumoniae ApxIA or ApxIIA in mice. Journal of veterinary science. 2007; 8(4); 383-392. [PubMed: 17993753].
Actacel
Vaccine Information
  • Vaccine Name: Actacel
  • Product Name: Diphtheria, tetanus, acellular pertussis, Haemophilus influenzae type b conjugate vaccine
  • Tradename: Actacel
  • Manufacturer: Sanofi Pasteur Ltd
  • Vaccine Ontology ID: VO_0010705
  • Type: Subunit vaccine
  • Status: Licensed
  • Location Licensed: Canada
  • Host Species for Licensed Use: Human
  • Adjuvant:
  • Preservative: 2 phenoxy ethanol
  • Immunization Route: Intramuscular injection (i.m.)
  • Storage: Refrigerate at 2° to 8°C.
  • Approved Age for Licensed Use: 2 months to 7 years
  • Description: Products: Proteins + Conjugate.
References
 
Actacel
Vaccine Information
  • Vaccine Name: Actacel
  • Tradename: Actacel
  • Manufacturer: Sanofi Pasteur Ltd
  • Vaccine Ontology ID: VO_0010705
  • Type: Subunit vaccine
  • Status: Licensed
  • Location Licensed: Canada
  • Host Species for Licensed Use: Human
  • Adjuvant:
  • Preservative: 2 phenoxy ethanol
  • Immunization Route: Intramuscular injection (i.m.)
  • Approved Age for Licensed Use: 2 months to 7 years
  • Description: Products: Proteins + Conjugate.
References
 
B. burgdorferi DbpA and OspA Protein Vaccine
Vaccine Information
  • Vaccine Name: B. burgdorferi DbpA and OspA Protein Vaccine
  • Vaccine Ontology ID: VO_0004188
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: DbpAN40-OspAN40
  • DbpA gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • OspA gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Adjuvant:
  • Immunization Route: Intraperitoneal injection (i.p.)
References
 
B. burgdorferi DbpA Protein Vaccine
Vaccine Information
References
Hanson et al., 2000: Hanson MS, Patel NK, Cassatt DR, Ulbrandt ND. Evidence for vaccine synergy between Borrelia burgdorferi decorin binding protein A and outer surface protein A in the mouse model of lyme borreliosis. Infection and immunity. 2000; 68(11); 6457-6460. [PubMed: 11035759].
B. burgdorferi OspA Protein Vaccine
Vaccine Information
  • Vaccine Name: B. burgdorferi OspA Protein Vaccine
  • Vaccine Ontology ID: VO_0004028
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: Recombinant OspA protein
  • OspA gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Adjuvant:
  • Immunization Route: Intraperitoneal injection (i.p.)
References
 
B. burgdorferi OspC Protein Vaccine
Vaccine Information
  • Vaccine Name: B. burgdorferi OspC Protein Vaccine
  • Vaccine Ontology ID: VO_0004030
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: Recombinant OspC protein
  • OspC gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Adjuvant:
  • Immunization Route: Intraperitoneal injection (i.p.)
References
 
B. melitensis P39 protein vaccine
Vaccine Information
  • Vaccine Name: B. melitensis P39 protein vaccine
  • Vaccine Ontology ID: VO_0000412
  • Type: Subunit vaccine
  • Antigen: Brucella melitensis 16M P39, a putative periplasmic binding protein (Al-Mariri et al., 2001).
  • B. melitensis M5 P39 gene engineering:
    • Type: recombinant protein
    • Description: The bfr gene of Brucella melitensis 16M was subcloned into a pET-15b expression vector that contains a polyhistidine tag, and the resulting plasmid pET-15b-bfr was introduced in E. coli BL21(DE3). After 2 to 4 of induction with 1 mM IPTG (isopropyl-β-d-thiogalactopyranoside), bacterial cells from a 100-ml culture were washed once and then sonicated. The lysate was centrifuged for 10 min at 9,000 × g at 4°C. The pellet was kept frozen at −70°C. After it had thawed, the pellet was resuspended in a lysis buffer. The resulting lysate was centrifuged at 9,000 × g for 20 min at 4°C (Al-Mariri et al., 2001). P39 was then purified based on metal chelate affinity chromatography as described previously (Letesson et al., 1997).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0001237
    • Description: The adjuvant is a synthetic phosphorothioate oligodeoxynucleotide containing an unmethylated, consensus immunostimulatory CpG motif (5′-purine-purine-CpG-pyrimidine-pyrimidine-3′ oligodeoxynucleotide [CpG ODN]). Specifically, the immunostimulatory CpG 1826 (5′-TCCATGACGTTCCTGACGTT-3′) was used (Al-Mariri et al., 2001).
  • Preparation: The bfr gene of Brucella melitensis 16M was subcloned and expressed in an expression vector. The protein was purified and mixed with the CpG ODN as the vaccine (Al-Mariri et al., 2001).
  • Virulence: Not reported.
  • Description: P39 has been found to be a Brucella protective antigen (Al-Mariri et al., 2001).
References
Al-Mariri et al., 2001: Al-Mariri A, Tibor A, Mertens P, De Bolle X, Michel P, Godefroid J, Walravens K, Letesson JJ. Protection of BALB/c mice against Brucella abortus 544 challenge by vaccination with bacterioferritin or P39 recombinant proteins with CpG oligodeoxynucleotides as adjuvant. Infection and immunity. 2001 Aug; 69(8); 4816-22. [PubMed: 11447155 ].
Letesson et al., 1997: Letesson JJ, Tibor A, van Eynde G, Wansard V, Weynants V, Denoel P, Saman E. Humoral immune responses of Brucella-infected cattle, sheep, and goats to eight purified recombinant Brucella proteins in an indirect enzyme-linked immunosorbent assay. Clinical and diagnostic laboratory immunology. 1997 Sep; 4(5); 556-64. [PubMed: 9302205].
B. pertussis CyaA protein vaccine
Vaccine Information
  • Vaccine Name: B. pertussis CyaA protein vaccine
  • Vaccine Ontology ID: VO_0011359
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: B. pertussis secreted adenylate cyclase (cyaA)
  • CyaA gene engineering:
    • Type: Recombinant protein preparation
    • Description: The AC was purified from culture supernatants using a camodulin affinity chromatography. The preparation consisted of two polypeptides of 45 and 43 kDa that are structurally related as described by Ladant et al (Guiso et al., 1989).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Subcutaneous injection
References
Guiso et al., 1989: Guiso N, Rocancourt M, Szatanik M, Alonso JM. Bordetella adenylate cyclase is a virulence associated factor and an immunoprotective antigen. Microbial pathogenesis. 1989; 7(5); 373-380. [PubMed: 2622329].
B. pertussis FhaB and 69 kDa OMP protein vaccine
Vaccine Information
  • Vaccine Name: B. pertussis FhaB and 69 kDa OMP protein vaccine
  • Vaccine Ontology ID: VO_0011498
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: Combination of the B. pertussis 69-kDa outer membrane protein and filamentous hemagglutinin (fhaB)
  • fhaB gene engineering:
    • Type: Recombinant protein preparation
    • Description: A crystal clear supernatant of 5-day-old static cultures containing proteolysis inhibitor was purified. To remove impurities, the FHA was precipitated by overnight dialysis against 25-30 volumes of buffer A at 4 C, and the precipitate was collected by centrifugation. The precipitated FHA was dissolved in the smallest possible volume of 40 mM B-alanine buffer at pH 3.5, clarified by centrifugation, and applied at room temperature at a flow of 30 ml/h to a Superose 12 column. The retained highly purified FHA was eluted (Novotny et al., 1991).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intramuscular injection (i.m.)
References
Novotny et al., 1991: Novotny P, Chubb AP, Cownley K, Charles IG. Biologic and protective properties of the 69-kDa outer membrane protein of Bordetella pertussis: a novel formulation for an acellular pertussis vaccine. The Journal of infectious diseases. 1991; 164(1); 114-122. [PubMed: 2056199].
B. pertussis PTx protein vaccine
Vaccine Information
  • Vaccine Name: B. pertussis PTx protein vaccine
  • Vaccine Ontology ID: VO_0011361
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: B. pertussis pertussis toxin (PTx)
  • ptxE gene engineering:
    • Type: Recombinant protein preparation
    • Description: Vaccine is prepared by chemically modifying purified PT from culture supernatants with tetranitromethane (TNM). The lot was adsorbed to aluminum hydroxide (Alhydogel; Superfos, Vedbaek, Denmark) at a concentration of 50 μg of protein adsorbed to 4 mg per 1.0 ml. Animal doses (2.5, 0.5, and 0.1 μg) were prepared by making fivefold serial dilutions in aluminum hydroxide (4 mg/ml) diluent and given in a volume of 50 μl (Bruss and Siber, 2002).
    • Detailed Gene Information: Click Here.
  • PtxA gene engineering:
    • Type: Recombinant protein preparation
    • Description: Vaccine is prepared by chemically modifying purified PT from culture supernatants with tetranitromethane (TNM). The lot was adsorbed to aluminum hydroxide (Alhydogel; Superfos, Vedbaek, Denmark) at a concentration of 50 μg of protein adsorbed to 4 mg per 1.0 ml. Animal doses (2.5, 0.5, and 0.1 μg) were prepared by making fivefold serial dilutions in aluminum hydroxide (4 mg/ml) diluent and given in a volume of 50 μl (Bruss and Siber, 2002).
    • Detailed Gene Information: Click Here.
  • ptxB gene engineering:
    • Type: Recombinant protein preparation
    • Description: Vaccine is prepared by chemically modifying purified PT from culture supernatants with tetranitromethane (TNM). The lot was adsorbed to aluminum hydroxide (Alhydogel; Superfos, Vedbaek, Denmark) at a concentration of 50 μg of protein adsorbed to 4 mg per 1.0 ml. Animal doses (2.5, 0.5, and 0.1 μg) were prepared by making fivefold serial dilutions in aluminum hydroxide (4 mg/ml) diluent and given in a volume of 50 μl (Bruss and Siber, 2002).
    • Detailed Gene Information: Click Here.
  • ptxC gene engineering:
    • Type: Recombinant protein preparation
    • Description: Vaccine is prepared by chemically modifying purified PT from culture supernatants with tetranitromethane (TNM). The lot was adsorbed to aluminum hydroxide (Alhydogel; Superfos, Vedbaek, Denmark) at a concentration of 50 μg of protein adsorbed to 4 mg per 1.0 ml. Animal doses (2.5, 0.5, and 0.1 μg) were prepared by making fivefold serial dilutions in aluminum hydroxide (4 mg/ml) diluent and given in a volume of 50 μl (Bruss and Siber, 2002).
    • Detailed Gene Information: Click Here.
  • ptxD gene engineering:
    • Type: Recombinant protein preparation
    • Description: Vaccine is prepared by chemically modifying purified PT from culture supernatants with tetranitromethane (TNM). The lot was adsorbed to aluminum hydroxide (Alhydogel; Superfos, Vedbaek, Denmark) at a concentration of 50 μg of protein adsorbed to 4 mg per 1.0 ml. Animal doses (2.5, 0.5, and 0.1 μg) were prepared by making fivefold serial dilutions in aluminum hydroxide (4 mg/ml) diluent and given in a volume of 50 μl (Bruss and Siber, 2002).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intraperitoneal injection (i.p.)
References
Bruss and Siber, 2002: Bruss JB, Siber GR. Quantitative priming with inactivated pertussis toxoid vaccine in the aerosol challenge model. Infection and immunity. 2002; 70(8); 4600-4608. [PubMed: 12117973].
Brucella ovis Microparticle Subunit Vaccine
Vaccine Information
  • Vaccine Name: Brucella ovis Microparticle Subunit Vaccine
  • Vaccine Ontology ID: VO_0004146
  • Type: Subunit vaccine
  • Antigen: A high hydrophobic antigenic complex taken from Brucella ovis (HS) (Estevan et al., 2006).
  • Adjuvant:
  • Preparation: The antigenic extract (HS) was obtained from B. ovis REO 198 cells. The bacterial cells were cultured, suspended in distilled water, and heat-killed in flowing steam. Following centrifugation, the supernatant was dialyzed against deionized water. The dialyzed material was ultracentrifuged, and the pellet (HS) was washed in dH2O and freeze-dried. The batch of antigen used to prepare the vaccine formulation contained 48.7 ± 5.0% protein and 41.7 ± 4.7% rough lipopolysaccharide (R-LPS). The vaccine consisted of F68–CD–MP microparticles suspended in saline. F68,CD, and MP are different excipients that were used in order to facilitate the encapsulation and conserve the bioactivity of the encapsulated antigenic complex (HS) (Estevan et al., 2006).
References
Estevan et al., 2006: Estevan M, Gamazo C, Grilló MJ, Del Barrio GG, Blasco JM, Irache JM. Experiments on a sub-unit vaccine encapsulated in microparticles and its efficacy against Brucella melitensis in mice. Vaccine. 2006; 24(19); 4179-4187. [PubMed: 16481077].
Brucella recombinant SurA protein vaccine
Vaccine Information
  • Vaccine Name: Brucella recombinant SurA protein vaccine
  • Vaccine Ontology ID: VO_0000358
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: The antigen for this vaccine is SurA protein from B. abortus strain 2308, B. abortus strain S19, and Brucella melitensis strain H38 (Delpino et al., 2007).
  • SurA gene engineering:
    • Type: Recombinant protein preparation
    • Description: Mice given rSurA with adjuvant exhibited a significant degree of protection against B. abortus infection (Delpino et al., 2007b).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000139
    • Description: Two different adjuvants were used in these vaccines: Complete Freund's Adjuvant (CFA) and Incomplete Freund's Adjuvant (IFA). CFA was administered on day 0 and IFA was administered on day 15 (Delpino et al., 2007).
  • Adjuvant:
    • VO ID: VO_0000142
    • Description: Two different adjuvants were used in these vaccines: Complete Freund's Adjuvant (CFA) and Incomplete Freund's Adjuvant (IFA). CFA was administered on day 0 and IFA was administered on day 15 (Delpino et al., 2007).
  • Preparation: The PCR primers for cloning SurA gene from B. abortus were as follows: sense 5′AGAAAGCATATGTTTGCAAGACCTCTT3′ (NdeI) and antisense 5′TCTTCGGGATCCTCAACGATTGACGATGGT3′ (BamHI). B. abortus genomic DNA was used as template for PCR with Pfu DNA polymerase (Stratagene). The surA gene was cloned to plasmid Pet17b and then transformed to E. coli JM19 and then BL21(DE3) competent cells. Recombinant proteins were adsorbed with Sepharose-polymyxin B (Sigma, St. Louis, MO) to eliminate lipopolysaccharide contamination. The antigen and PBS were administered mixed with Complete Freund's Adjuvant (CFA) (Sigma) on day 0 and with Incomplete Freund's Adjuvant (IFA) on day 15 (Delpino et al., 2007).
  • Immunization Route: Nasal spray, Intraperitoneal injection (i.p.)
References
Delpino et al., 2007b: Delpino MV, Estein SM, Fossati CA, Baldi PC, Cassataro J. Vaccination with Brucella recombinant DnaK and SurA proteins induces protection against Brucella abortus infection in BALB/c mice. Vaccine. 2007; 25(37-38); 6721-6729. [PubMed: 17686554].
C. jejuni FlaC protein vaccine
Vaccine Information
  • Vaccine Name: C. jejuni FlaC protein vaccine
  • Vaccine Ontology ID: VO_0011495
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: C. jejuni flagellin subunit protein FlaC
  • FlaC gene engineering:
    • Type: Recombinant protein preparation
    • Description: The flaC gene from C. jejuni 81-176 was expressed in Escherichia coli as hexahistidine-tagged proteins in pET-19b. Strains of BL21(DE3) containing each clone were grown in Luria broth containing 100 μg/ml ampicillin and proteins were purified by nickel chromatography under native conditions (Baqar et al., 2008).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intranasal
References
Baqar et al., 2008: Baqar S, Applebee LA, Gilliland TC Jr, Lee LH, Porter CK, Guerry P. Immunogenicity and protective efficacy of recombinant Campylobacter jejuni flagellum-secreted proteins in mice. Infection and immunity. 2008; 76(7); 3170-3175. [PubMed: 18426878].
C. jejuni FspA1 protein vaccine
Vaccine Information
  • Vaccine Name: C. jejuni FspA1 protein vaccine
  • Vaccine Ontology ID: VO_0011485
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: C. jejuni flagellum-secreted protein FspA1
  • fspA1 gene engineering:
    • Type: Recombinant protein preparation
    • Description: The fspA1 gene from C. jejuni 81-176 was expressed in Escherichia coli as hexahistidine-tagged proteins in pET-19b. Strains of BL21(DE3) containing each clone were grown in Luria broth containing 100 μg/ml ampicillin and proteins were purified by nickel chromatography under native conditions (Baqar et al., 2008).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intranasal
References
Baqar et al., 2008: Baqar S, Applebee LA, Gilliland TC Jr, Lee LH, Porter CK, Guerry P. Immunogenicity and protective efficacy of recombinant Campylobacter jejuni flagellum-secreted proteins in mice. Infection and immunity. 2008; 76(7); 3170-3175. [PubMed: 18426878].
C. jejuni FspA2 protein vaccine
Vaccine Information
  • Vaccine Name: C. jejuni FspA2 protein vaccine
  • Vaccine Ontology ID: VO_0011487
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: C. jejuni flagellum-secreted protein FspA2
  • fspA2 gene engineering:
    • Type: Recombinant protein preparation
    • Description: The fspA2 gene from C. jejuni CG8486 were expressed in Escherichia coli as hexahistidine-tagged proteins in pET-19b. Strains of BL21(DE3) containing each clone were grown in Luria broth containing 100 μg/ml ampicillin and proteins were purified by nickel chromatography under native conditions (Baqar et al., 2008).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intranasal
References
Baqar et al., 2008: Baqar S, Applebee LA, Gilliland TC Jr, Lee LH, Porter CK, Guerry P. Immunogenicity and protective efficacy of recombinant Campylobacter jejuni flagellum-secreted proteins in mice. Infection and immunity. 2008; 76(7); 3170-3175. [PubMed: 18426878].
C. jejuni MBP-FlaA protein vaccine
Vaccine Information
  • Vaccine Name: C. jejuni MBP-FlaA protein vaccine
  • Vaccine Ontology ID: VO_0011493
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: C. jejuni structural flagella protein flaA and maltose-binding protein MBP
  • FlaA from C. jejuni 81-176 gene engineering:
    • Type: Recombinant protein preparation
    • Description: Purification schemes were essentially as recommended by NEB. DH5α containing the flagellin-MBP fusion was grown overnight in 10 ml of rich medium (10 g of tryptone, 5 g of yeast extract, 5 g of NaCl, and 2 g of glucose/liter) supplemented with 100 μg of ampicillin per ml and used to inoculate a fresh 1-liter culture of the same medium. This culture was grown with shaking at 37°C to an optical density at 600 nm of 0.5, and IPTG (isopropyl-β-d-thiogalactoside; Gibco, Gaithersburg, Md.) was added to a final concentration of 0.3 mM (Lee et al., 1999).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intranasal
References
Lee et al., 1999: Lee LH, Burg E 3rd, Baqar S, Bourgeois AL, Burr DH, Ewing CP, Trust TJ, Guerry P. Evaluation of a truncated recombinant flagellin subunit vaccine against Campylobacter jejuni. Infection and immunity. 1999 Nov; 67(11); 5799-805. [PubMed: 10531231].
C. jejuni PorA protein vaccine
Vaccine Information
  • Vaccine Name: C. jejuni PorA protein vaccine
  • Vaccine Ontology ID: VO_0004203
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: Recombinant PorA protein
  • PorA gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: orally
References
 
C. muridarum MOMP protein vaccine
Vaccine Information
  • Vaccine Name: C. muridarum MOMP protein vaccine
  • Vaccine Ontology ID: VO_0011453
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: C. muridarum major outer membrane protein MOMP
  • MOMP gene engineering:
    • Type: Recombinant protein preparation
    • Description: Recombinant maltose binding protein-MOMP (MBP-MOMP) was cloned into the bacterial expression vector pMAL-c2, and used to transform Escherichia coli (DH5α[pMMM3]). The MBP-MOMP was purified by passage through a PD-10 column (Amersham Biosciences, NSW, Australia), followed by a Sephadex G-75 column (Sigma–Aldrich) (Skelding et al., 2006).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Adjuvant:
  • Immunization Route: Intranasal immunization
References
Skelding et al., 2006: Skelding KA, Hickey DK, Horvat JC, Bao S, Roberts KG, Finnie JM, Hansbro PM, Beagley KW. Comparison of intranasal and transcutaneous immunization for induction of protective immunity against Chlamydia muridarum respiratory tract infection. Vaccine. 2006; 24(3); 355-366. [PubMed: 16153755].
C. muridarum PmpE/F-2 protein vaccine
Vaccine Information
  • Vaccine Name: C. muridarum PmpE/F-2 protein vaccine
  • Vaccine Ontology ID: VO_0011456
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: C. muridarum polymorphic membrane protein E/F family protein
  • PmpE/F-2 gene engineering:
    • Type: Recombinant protein preparation
    • Description: The source proteins containing the MHC II binding Chlamydia peptides were cloned, expressed and purified as follows: pmpE/F-2 and gap DNA fragments were generated by PCR using genomic DNA isolated from C. muridarum. The PCR products were purified and cloned into pET32a (Novagen) for pmpE/F-2 and gap after restriction enzyme digestion with BamHI/NotI using standard molecular biology techniques. Only the first half of the gene (25–575) was cloned into the vector for expression (Yu et al., 2009).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000142
    • Description: Incomplete Freunds Adjuvant (Sigma)
  • Immunization Route: Intravenous injection (i.v.)
References
Yu et al., 2009: Yu H, Jiang X, Shen C, Karunakaran KP, Brunham RC. Novel Chlamydia muridarum T cell antigens induce protective immunity against lung and genital tract infection in murine models. Journal of immunology (Baltimore, Md. : 1950). 2009; 182(3); 1602-1608. [PubMed: 19155509].
C. muridarum PmpG-1 protein vaccine
Vaccine Information
  • Vaccine Name: C. muridarum PmpG-1 protein vaccine
  • Vaccine Ontology ID: VO_0011458
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: C. muridarum polymorphic membrane protein G family protein
  • PmpG-1 gene engineering:
    • Type: Recombinant protein preparation
    • Description: The source proteins containing the MHC II binding Chlamydia peptides were cloned, expressed and purified as follows: pmpG-1 and gap DNA fragments were generated by PCR using genomic DNA isolated from C. muridarum. The PCR products were purified and cloned into pET32a (Novagen) for pmpG-1 and gap after restriction enzyme digestion with BamHI/NotI using standard molecular biology techniques. Only the first half of the gene (25–500) was cloned into the vector for expression (Yu et al., 2009).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000142
    • Description: Incomplete Freunds Adjuvant (Sigma)
  • Immunization Route: Intravenous injection (i.v.)
References
Yu et al., 2009: Yu H, Jiang X, Shen C, Karunakaran KP, Brunham RC. Novel Chlamydia muridarum T cell antigens induce protective immunity against lung and genital tract infection in murine models. Journal of immunology (Baltimore, Md. : 1950). 2009; 182(3); 1602-1608. [PubMed: 19155509].
C. muridarum PmpG-1, PmpE/F-2, and MOMP Proteins Vaccine
Vaccine Information
References
Yu et al., 2010: Yu H, Jiang X, Shen C, Karunakaran KP, Jiang J, Rosin NL, Brunham RC. Chlamydia muridarum T-cell antigens formulated with the adjuvant DDA/TDB induce immunity against infection that correlates with a high frequency of gamma interferon (IFN-gamma)/tumor necrosis factor alpha and IFN-gamma/interleukin-17 double-positive CD4+ T cells. Infection and immunity. 2010; 78(5); 2272-2282. [PubMed: 20231405].
C. muridarum RplF protein vaccine
Vaccine Information
  • Vaccine Name: C. muridarum RplF protein vaccine
  • Vaccine Ontology ID: VO_0011437
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: C. muridarum rplF
  • RplF gene engineering:
    • Type: Recombinant protein preparation
    • Description: The source proteins containing the MHC II binding Chlamydia peptides were cloned, expressed and purified as follows: rplF DNA fragments were generated by PCR using genomic DNA isolated from C. muridarum. The PCR products were purified and cloned into pGEX-6P-3 (GE Healthcare) after restriction enzyme digestion with BamHI/NotI using standard molecular biology techniques (Yu et al., 2009).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000142
    • Description: Incomplete Freunds Adjuvant (Sigma)
  • Immunization Route: Intravenous injection (i.v.)
References
Yu et al., 2009: Yu H, Jiang X, Shen C, Karunakaran KP, Brunham RC. Novel Chlamydia muridarum T cell antigens induce protective immunity against lung and genital tract infection in murine models. Journal of immunology (Baltimore, Md. : 1950). 2009; 182(3); 1602-1608. [PubMed: 19155509].
C. muridarum Tarp subunit vaccine
Vaccine Information
  • Vaccine Name: C. muridarum Tarp subunit vaccine
  • Vaccine Ontology ID: VO_0004202
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: purified C. muridarum Tarp
  • Tarp gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Adjuvant:
  • Immunization Route: Intramuscular injection (i.m.)
References
 
C. pneumoniae CopN protein vaccine
Vaccine Information
  • Vaccine Name: C. pneumoniae CopN protein vaccine
  • Vaccine Ontology ID: VO_0011432
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: C. pneumoniae copN
  • copN gene engineering:
    • Type: Recombinant protein preparation
    • Description: C. pneumoniae CopN (gene lcrE; position 0324 of C. pneumoniae CWL029), was produced in a Bacillus subtilis protein expression system as a soluble protein. Recombinant CopN protein was dissolved in PBS at a concentration of 1 mg/ml and heated to 100 °C for 10 min after which the visible precipitation of protein was discernible. C. pneumoniae preparation was boiled for 10 min in a water bath at a concentration of 2.5 × 10^7 IFU/ml in SPG. E. coli heat-labile toxin, LT (kindly provided by Prof. G. Dougan, Imperial Collage, London, UK) was added to heat-aggregated protein suspension to a final concentration of 12.5 μg/ml (Tammiruusu et al., 2007).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intranasal
References
Tammiruusu et al., 2007: Tammiruusu A, Penttilä T, Lahesmaa R, Sarvas M, Puolakkainen M, Vuola JM. Intranasal administration of chlamydial outer protein N (CopN) induces protection against pulmonary Chlamydia pneumoniae infection in a mouse model. Vaccine. 2007; 25(2); 283-290. [PubMed: 16949182].
C. pneumoniae LcrE protein vaccine
Vaccine Information
  • Vaccine Name: C. pneumoniae LcrE protein vaccine
  • Vaccine Ontology ID: VO_0011435
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: C. pneumoniae LcrE
  • LcrE gene engineering:
    • Type: Recombinant protein preparation
    • Description: A 1218-kb DNA fragment containing the lcrE gene (GenBank ID 15618244, Locus tag CPn0324) was amplified by PCR, using C. pneumoniae (CWL029 ATCC) DNA as template. The PCR was performed in a GeneAmp II (Applied Biosystems, Foster City, CA, USA) thermocycler with Advantage GC cDNA polymerase (Clontech, Mountain View, CA, USA), and the amplification conditions were set as recommended by the manufacturer. The amplicon was digested with NdeI and BamHI and inserted into p6HisF-11d (icl) pET vector by digesting it with the same enzymes and replacing the icl gene (Faludi et al., 2009).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000884
    • Description: Either Freund's or Alum adjuvants
  • Adjuvant:
  • Immunization Route: Subcutaneous injection
References
Faludi et al., 2009: Faludi I, Burian K, Csanadi A, Miczak A, Lu X, Kakkar VV, Gonczol E, Endresz V. Adjuvant modulation of the immune response of mice against the LcrE protein of Chlamydophila pneumoniae. International journal of medical microbiology : IJMM. 2009; 299(7); 520-528. [PubMed: 19451031].
E. coli CS3 in PLGA microspheres
Vaccine Information
References
Byrd and Cassels, 2006: Byrd W, Cassels FJ. The encapsulation of enterotoxigenic Escherichia coli colonization factor CS3 in biodegradable microspheres enhances the murine antibody response following intranasal administration. Microbiology (Reading, England). 2006; 152(Pt 3); 779-786. [PubMed: 16514157].
E. coli Escheriosome-mediated Cytosolic Delivery of recombinant Brucella rL7/L12 Protein
Vaccine Information
References
Mallick et al., 2007: Mallick AI, Singha H, Khan S, Anwar T, Ansari MA, Khalid R, Chaudhuri P, Owais M. Escheriosome-mediated delivery of recombinant ribosomal L7/L12 protein confers protection against murine brucellosis. Vaccine. 2007; 25(46); 7873-7884. [PubMed: 17931756].
E. coli Hma protein vaccine
Vaccine Information
  • Vaccine Name: E. coli Hma protein vaccine
  • Vaccine Ontology ID: VO_0011443
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: E. coli outer membrane receptor for iron compound or colicin (Hma)
  • Hma gene engineering:
    • Type: Recombinant protein preparation
    • Description: Genes encoding the selected antigens were PCR-amplified from CFT073 genomic DNA and cloned into either pBAD-myc-HisA (Invitrogen) or pET30b+ (Novagen). The six iron receptor vaccine candidates, ChuA, Hma, IutA, IreA, Iha, and IroN were expressed and purified as affinity-tagged recombinant proteins. Consistent with the predicted structure of these antigens, the CD spectrum of refolded purified Hma displayed a trough at 218 nm, which is characteristic of a β-sheet-rich conformation. The six purified protein antigens were each biochemically cross-linked to the adjuvant cholera toxin (CT) at a ratio of 10:1 (Alteri et al., 2009).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intranasal
References
Alteri et al., 2009: Alteri CJ, Hagan EC, Sivick KE, Smith SN, Mobley HL. Mucosal immunization with iron receptor antigens protects against urinary tract infection. PLoS pathogens. 2009; 5(9); e1000586. [PubMed: 19806177].
E. coli IreA protein vaccine
Vaccine Information
  • Vaccine Name: E. coli IreA protein vaccine
  • Vaccine Ontology ID: VO_0011444
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: E. coli iron-regulated outer membrane virulence protein (IreA)
  • ireA gene engineering:
    • Type: Recombinant protein preparation
    • Description: Genes encoding the selected antigens were PCR-amplified from CFT073 genomic DNA and cloned into either pBAD-myc-HisA (Invitrogen) or pET30b+ (Novagen). The six iron receptor vaccine candidates, ChuA, Hma, IutA, IreA, Iha, and IroN were expressed and purified as affinity-tagged recombinant proteins. Consistent with the predicted structure of these antigens, the CD spectrum of refolded purified Hma displayed a trough at 218 nm, which is characteristic of a β-sheet-rich conformation. The six purified protein antigens were each biochemically cross-linked to the adjuvant cholera toxin (CT) at a ratio of 101 (Alteri et al., 2009).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intranasal
References
Alteri et al., 2009: Alteri CJ, Hagan EC, Sivick KE, Smith SN, Mobley HL. Mucosal immunization with iron receptor antigens protects against urinary tract infection. PLoS pathogens. 2009; 5(9); e1000586. [PubMed: 19806177].
E. coli IutA protein vaccine
Vaccine Information
  • Vaccine Name: E. coli IutA protein vaccine
  • Vaccine Ontology ID: VO_0011445
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: E. coli IutA
  • iutA gene engineering:
    • Type: Recombinant protein preparation
    • Description: Genes encoding the selected antigens were PCR-amplified from CFT073 genomic DNA and cloned into either pBAD-myc-HisA (Invitrogen) or pET30b+ (Novagen). The six iron receptor vaccine candidates, ChuA, Hma, IutA, IreA, Iha, and IroN were expressed and purified as affinity-tagged recombinant proteins. Consistent with the predicted structure of these antigens, the CD spectrum of refolded purified Hma displayed a trough at 218 nm, which is characteristic of a β-sheet-rich conformation. The six purified protein antigens were each biochemically cross-linked to the adjuvant cholera toxin (CT) at a ratio of 10:1 (Alteri et al., 2009).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intranasal
References
Alteri et al., 2009: Alteri CJ, Hagan EC, Sivick KE, Smith SN, Mobley HL. Mucosal immunization with iron receptor antigens protects against urinary tract infection. PLoS pathogens. 2009; 5(9); e1000586. [PubMed: 19806177].
E. coli O157:H7 intimin vaccine
Vaccine Information
  • Vaccine Name: E. coli O157:H7 intimin vaccine
  • Vaccine Ontology ID: VO_0000110
  • Type: Subunit vaccine
  • Antigen: The antigen used in this vaccine was Int280α, which is the recombinant LEE-encoded protein from EPEC strain E2348/69. Int280α, a specific type of intimin, is the target of long-lived humoral immune responses in C. rodentium-infected mice. (Ghaem-Maghami et al., 2001).
  • Adjuvant:
  • Preparation: A highly purified preparation of recombinant Int280α from EPEC E2348/69 was used as an immunogen in mucosal and parenteral vaccination regimes (Ghaem-Maghami et al., 2001).
References
Ghaem-Maghami et al., 2001: Ghaem-Maghami M, Simmons CP, Daniell S, Pizza M, Lewis D, Frankel G, Dougan G. Intimin-specific immune responses prevent bacterial colonization by the attaching-effacing pathogen Citrobacter rodentium. Infection and immunity. 2001; 69(9); 5597-5605. [PubMed: 11500434 ].
E. coli O157:H7 subunit vaccine expressing Esps and Tir
Vaccine Information
  • Vaccine Name: E. coli O157:H7 subunit vaccine expressing Esps and Tir
  • Vaccine Ontology ID: VO_0000459
  • Type: Subunit vaccine
  • Antigen: The antigen for this vaccine is supernatant proteins (containing Type III proteins Esps and Tir) prepared from E. Coli O157-H7 (Potter et al., 2004).
  • Tir gene engineering:
    • Type: Protein purification
    • Description: The E. coli strain O157:H7 was used for the production of Type III secreted proteins Tir and Esps (Potter et al., 2004).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Preparation: Supernatent proteins from E. coli O157-H7 were combined with the VSA3 to form protein concentrations of either 25 or 100 micrograms/ml. Each dose was 50 micrograms/ml (Potter et al., 2004).
  • Virulence: Not noted.
References
Potter et al., 2004: Potter AA, Klashinsky S, Li Y, Frey E, Townsend H, Rogan D, Erickson G, Hinkley S, Klopfenstein T, Moxley RA, Smith DR, Finlay BB. Decreased shedding of Escherichia coli O157:H7 by cattle following vaccination with type III secreted proteins. Vaccine. 2004; 22(3-4); 362-369. [PubMed: 14670317].
E. coli vaccine based on recombinant protein CO393
Vaccine Information
  • Vaccine Name: E. coli vaccine based on recombinant protein CO393
  • Tradename: None
  • Vaccine Ontology ID: VO_0000485
  • Type: Subunit vaccine
  • Antigen: C0393 protein associated with ExPEC strains (Durant et al., 2007).
  • C0393 gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000139
    • Description: Recombinant protein was emulsified in complete Freund's adjuvant (Sigma) during innoculation, but emulsified in incomplete Freund's adjuvant during boosting (Durant et al., 2007).
  • Adjuvant:
    • VO ID: VO_0000142
    • Description: Recombinant protein was emulsified in complete Freund's adjuvant (Sigma) during innoculation, but emulsified in incomplete Freund's adjuvant during boosting (Durant et al., 2007).
  • Preparation: The chromosomal DNA of strain S26 was used as the source of DNA for expression of predicted surface antigens. PCR was performed. After purification, the PCR products were introduced into plasmid expression vectors to generate proteins fused with His6. The resulting plasmids were introduced into E. coli BL21 Star (DE3) (Invitrogen, Carlsbad, CA). For protein expression, overnight cultures were used to inoculate a fresh LB medium supplemented with ampicillin (100 µg/ml). Bacteria were grown and then harvested by centrifugation. Purification of recombinant proteins was performed by affinity chromatography . Fractions containing the recombinant protein were pooled and concentrated (Durant et al., 2007).
  • Virulence: Not noted.
  • Description: In terms of biological significance to humans, E. coli strains are grouped into three categories: (i) commensal strains that represent a large part of the normal flora, (ii) intestinal pathogenic strains that cause diseases when ingested in sufficient quantities, and (iii) pathogenic strains causing extraintestinal infections (extraintestinal pathogenic E. coli [ExPEC]). Recently, the resistance of the ExPEC strains to various classes of antibiotics has become a major concern both in hospitals and in the community. Vaccines represent a rational alternative approach for the prevention of these infections. In this case, the challenge is to selectively prevent a subtype of E. coli strains that is not normally part of the commensal flora. Therefore, it is of great importance to find some specific genetic traits of these ExPEC strains. The current study identifies putative antigens from ExPEC-specific genomic sequences. In an animal model of lethal sepsis, the protective effect of immunization with these antigens was demonstrated, allowing the identification of five antigens as vaccine candidates against an extraintestinal E. coli infection (Durant et al., 2007).
References
Durant et al., 2007: Durant L, Metais A, Soulama-Mouze C, Genevard JM, Nassif X, Escaich S. Identification of candidates for a subunit vaccine against extraintestinal pathogenic Escherichia coli. Infection and immunity. 2007 Apr; 75(4); 1916-25. [PubMed: 17145948 ].
E. coli vaccine based on recombinant protein FyuA
Vaccine Information
  • Vaccine Name: E. coli vaccine based on recombinant protein FyuA
  • Tradename: None
  • Vaccine Ontology ID: VO_0000485
  • Type: Subunit vaccine
  • Antigen: FyuA protein associated with ExPEC strains (Durant et al., 2007).
  • FyuA gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000139
    • Description: Recombinant protein was emulsified in complete Freund's adjuvant (Sigma) during innoculation, but emulsified in incomplete Freund's adjuvant during boosting (Durant et al., 2007).
  • Adjuvant:
    • VO ID: VO_0000142
    • Description: Recombinant protein was emulsified in complete Freund's adjuvant (Sigma) during innoculation, but emulsified in incomplete Freund's adjuvant during boosting (Durant et al., 2007).
  • Preparation: The chromosomal DNA of strain S26 was used as the source of DNA for expression of predicted surface antigens. PCR was performed. After purification, the PCR products were introduced into plasmid expression vectors to generate proteins fused with His6. The resulting plasmids were introduced into E. coli BL21 Star (DE3) (Invitrogen, Carlsbad, CA). For protein expression, overnight cultures were used to inoculate a fresh LB medium supplemented with ampicillin (100 µg/ml). Bacteria were grown and then harvested by centrifugation. Purification of recombinant proteins was performed by affinity chromatography . Fractions containing the recombinant protein were pooled and concentrated (Durant et al., 2007).
  • Virulence: Not noted.
  • Description: In terms of biological significance to humans, E. coli strains are grouped into three categories: (i) commensal strains that represent a large part of the normal flora, (ii) intestinal pathogenic strains that cause diseases when ingested in sufficient quantities, and (iii) pathogenic strains causing extraintestinal infections (extraintestinal pathogenic E. coli [ExPEC]). Recently, the resistance of the ExPEC strains to various classes of antibiotics has become a major concern both in hospitals and in the community. Vaccines represent a rational alternative approach for the prevention of these infections. In this case, the challenge is to selectively prevent a subtype of E. coli strains that is not normally part of the commensal flora. Therefore, it is of great importance to find some specific genetic traits of these ExPEC strains. The current study identifies putative antigens from ExPEC-specific genomic sequences. In an animal model of lethal sepsis, the protective effect of immunization with these antigens was demonstrated, allowing the identification of five antigens as vaccine candidates against an extraintestinal E. coli infection (Durant et al., 2007).
References
Durant et al., 2007: Durant L, Metais A, Soulama-Mouze C, Genevard JM, Nassif X, Escaich S. Identification of candidates for a subunit vaccine against extraintestinal pathogenic Escherichia coli. Infection and immunity. 2007 Apr; 75(4); 1916-25. [PubMed: 17145948 ].
E. coli vaccine using intimin polypeptide
Vaccine Information
  • Vaccine Name: E. coli vaccine using intimin polypeptide
  • Tradename: None
  • Vaccine Ontology ID: VO_0000478
  • Type: Subunit vaccine
  • Antigen: E. coli Intimin polypeptide(van et al., 2007).
  • eae gene engineering:
    • Type: Preparation of recombinant protein
    • Description: The portion of the eae gene that encodes the carboxyl-terminal 280 amino acids of intimin was amplified by polymerase chain reaction from EHEC O26:H- strain 193 (Int280-β) and EHEC O157:H7 strain EDL933 (Int280-γ) using a conserved forward primer (Int-LIC-for: 5′-GAC GAC GAC AAG ATT ACT GAG ATT AAG GCT G-3′) and subtype-specific reverse primers (O26Int-LIC-rev: 5′-GAG GAG AAG CCC GGT TTA TTT TAC ACA AAC AG-3′ and O157Int-LIC-rev: 5′-GAG GAG AAG CCC GGT TTA TTC TAC ACA AAC CG-3′). The products were cloned in pET30-Ek/Lic (Novagen®) by a ligation-independent method as amino-terminal 6×His-S-tag fusions. Proteins were expressed in E. coli K-12 strain BL21 (DE3) Star cells which lack RNaseE to stabilise mRNA. The Overnight Express™ Autoinduction System I (Novagen®) was used to induce Int280-γ and Int280-β expression. Cell extracts were prepared using BugBuster® (Novagen®) and the supernatant fraction mixed with His-Mag™ Agarose Beads (Novagen®) for affinity purification of the Int280 proteins as described by the manufacturer
      (van et al., 2007).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000127
    • Description: Aluminium hydroxide oil-based adjuvant (Alu-Oil; Intervet International BV, Boxmeer, The Netherlands) (van et al., 2007).
  • Preparation: Proteins were expressed in E. coli K-12 strain BL21 (DE3) Star cells which lack RNaseE to stabilise mRNA. The Overnight Express™ Autoinduction System I (Novagen®) was used to induce Int280-γ and Int280-β expression. Cell extracts were prepared using BugBuster® (Novagen®) and the supernatant fraction mixed with His-Mag™ Agarose Beads (Novagen®) for affinity purification of the Int280 proteins as described by the manufacturer (van et al., 2007).
  • Virulence: Not noted.
  • Description: Enterohaemorrhagic Escherichia coli (EHEC) are zoonotic enteric pathogens of worldwide importance. EHEC strains produce intimin, an outer membrane adhesin encoded by the eae gene located in a chromosomal pathogenicity island termed the locus of enterocyte effacement (LEE). Intimin mediates intimate bacterial attachment to enterocytes by binding to Tir, a bacterial protein which is translocated into host cells by a LEE-encoded type III secretion system. Intimin can also bind in vitro to β1-integrins and cell-surface localised nucleolin and these proteins can be detected proximal to adherent EHEC O157:H7 in vivo. Intimin is a key colonisation factor for EHEC O157:H7 in neonatal calves, young and weaned calves, and adult cattle and sheep. In addition, intimin influences the carriage and virulence of EHEC O157:H7 in streptomycin pre-treated mice, infant rabbits, and gnotobiotic and neonatal piglets (van et al., 2007).
References
van et al., 2007: van Diemen PM, Dziva F, Abu-Median A, Wallis TS, van den Bosch H, Dougan G, Chanter N, Frankel G, Stevens MP. Subunit vaccines based on intimin and Efa-1 polypeptides induce humoral immunity in cattle but do not protect against intestinal colonisation by enterohaemorrhagic Escherichia coli O157:H7 or O26:H-. Veterinary immunology and immunopathology. 2007 Mar 15; 116(1-2); 47-58. [PubMed: 17258324].
E. coli vaccine using verocytotoxin toxoid
Vaccine Information
  • Vaccine Name: E. coli vaccine using verocytotoxin toxoid
  • Vaccine Ontology ID: VO_0000501
  • Type: Subunit vaccine
  • Antigen: The antigens for these vaccines are either verocytoxin 1 (VT1) or verocytoxin 2 (VT2). The prototype toxin VT1 is virtually identical to Shiga toxin produced by Shigella dysenteriae type 1. By using in vitro neutralization tests in Vero cells, VT1 has been shown to be serologically distinct from VT2 in that these toxins showed no cross-neutralization by heterologous antisera (Bielaszewska et al., 1997).
  • Adjuvant:
    • VO ID: VO_0000142
    • Description: Freund’s incomplete adjuvant was used in the making of these vaccines (Bielaszewska et al., 1997).
  • Preparation: VT1 was purified from JB28, an E. coli TB1 strain. VT2 was purified from E. coli R82pJES 120DH5a. The purity of these toxin preparations was established by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoretic analysis. The labeled toxins were characterized for specific activity (1.7 x 10^5 to 2.3 x 10^5 cpm/mg) and biological activity (3.8 x 10^5 and 1.9 x 10^3 50% cytotoxic doses [CD50s]/mg for VT1 and VT2, respectively). The Vero cell binding activities, which represent the percentage of the input activity bound to the 25-sq cm monolayers after 1h of incubation and three washes, were 48% for VT2 preparations and 75% for VT1 preparations. For the subunit immunizations, VT1 and VT2 were separated into the A and B subunit fractions by SDS-polyacrylamide gel electrophoresis. (Bielaszewska et al., 1997).
References
Bielaszewska et al., 1997: Bielaszewska M, Clarke I, Karmali MA, Petric M. Localization of intravenously administered verocytotoxins (Shiga-like toxins) 1 and 2 in rabbits immunized with homologous and heterologous toxoids and toxin subunits. Infection and immunity. 1997; 65(7); 2509-2516. [PubMed: 9199412].
E.coli vaccine based on recombinant protein IroN
Vaccine Information
  • Vaccine Name: E.coli vaccine based on recombinant protein IroN
  • Tradename: None
  • Vaccine Ontology ID: VO_0000481
  • Type: Subunit vaccine
  • Antigen: IroN protein associated with ExPEC strains (Durant et al., 2007).
  • Adjuvant:
    • VO ID: VO_0000139
    • Description: Recombinant protein was emulsified in complete Freund's adjuvant (Sigma) during innoculation, but emulsified in incomplete Freund's adjuvant during boosting (Durant et al., 2007).
  • Adjuvant:
    • VO ID: VO_0000142
    • Description: Recombinant protein was emulsified in complete Freund's adjuvant (Sigma) during innoculation, but emulsified in incomplete Freund's adjuvant during boosting (Durant et al., 2007).
  • Preparation: The chromosomal DNA of strain S26 was used as the source of DNA for expression of predicted surface antigens. PCR was performed. After purification, the PCR products were introduced into plasmid expression vectors to generate proteins fused with His6. The resulting plasmids were introduced into E. coli BL21 Star (DE3) (Invitrogen, Carlsbad, CA). For protein expression, overnight cultures were used to inoculate a fresh LB medium supplemented with ampicillin (100 µg/ml). Bacteria were grown and then harvested by centrifugation. Purification of recombinant proteins was performed by affinity chromatography . Fractions containing the recombinant protein were pooled and concentrated (Durant et al., 2007).
  • Virulence: Not noted.
  • Description: In terms of biological significance to humans, E. coli strains are grouped into three categories: (i) commensal strains that represent a large part of the normal flora, (ii) intestinal pathogenic strains that cause diseases when ingested in sufficient quantities, and (iii) pathogenic strains causing extraintestinal infections (extraintestinal pathogenic E. coli [ExPEC]). Recently, the resistance of the ExPEC strains to various classes of antibiotics has become a major concern both in hospitals and in the community. Vaccines represent a rational alternative approach for the prevention of these infections. In this case, the challenge is to selectively prevent a subtype of E. coli strains that is not normally part of the commensal flora. Therefore, it is of great importance to find some specific genetic traits of these ExPEC strains. The current study identifies putative antigens from ExPEC-specific genomic sequences. In an animal model of lethal sepsis, the protective effect of immunization with these antigens was demonstrated, allowing the identification of five antigens as vaccine candidates against an extraintestinal E. coli infection (Durant et al., 2007).
References
Durant et al., 2007: Durant L, Metais A, Soulama-Mouze C, Genevard JM, Nassif X, Escaich S. Identification of candidates for a subunit vaccine against extraintestinal pathogenic Escherichia coli. Infection and immunity. 2007 Apr; 75(4); 1916-25. [PubMed: 17145948 ].
EHEC O157 subunit vaccine using his-tagged N-terminal intimin
Vaccine Information
  • Vaccine Name: EHEC O157 subunit vaccine using his-tagged N-terminal intimin
  • Vaccine Ontology ID: VO_0000505
  • Type: Subunit vaccine
  • Antigen: The antigen used in this vaccine was purified intimin O157, creating antibodies against EHEC O157 adhesin (Dean-Nystrom et al., 2002).
  • CS1 gene engineering:
    • Type: Gene mutation
    • Description: RIHisEae is a histidine-tagged version of the entire intimin protein from EHEC O157:H7 strain 86-24 minus the N-terminal 35 amino acids, which are thought to be part of a cleaved N-terminal signal sequence. For analysis of colostrum samples, a histidine-tagged N-terminal two-thirds fragment of intimin and a histidine-tagged C-terminal one-third fragment of intimin were purified (Dean-Nystrom et al., 2002).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Preparation: The histidine-tagged intimin O157 protein RIHisEae was purified. RIHisEae is a histidine-tagged version of the entire intimin protein from EHEC O157:H7 strain 86-24 minus the N-terminal 35 amino acids, which are thought to be part of a cleaved N-terminal signal sequence. The intimin was mixed with TiterMax Gold to form the vaccine (Dean-Nystrom et al., 2002).
References
Dean-Nystrom et al., 2002: Dean-Nystrom EA, Gansheroff LJ, Mills M, Moon HW, O'Brien AD. Vaccination of pregnant dams with intimin(O157) protects suckling piglets from Escherichia coli O157:H7 infection. Infection and immunity. 2002; 70(5); 2414-2418. [PubMed: 11953378].
F. tularensis FopB Protein Vaccine
Vaccine Information
  • Vaccine Name: F. tularensis FopB Protein Vaccine
  • Vaccine Ontology ID: VO_0004034
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: .5 μg recombinant FopB protein
  • FopB gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0001237
    • Description: 10 μg of CpG oligodeoxynucleotide (5′-TCCATGACGTTCCTGACGTT-3′; Operon, Huntsville, AL)
  • Immunization Route: intranasal immunization
References
 
F. tularensis GroEL protein vaccine
Vaccine Information
  • Vaccine Name: F. tularensis GroEL protein vaccine
  • Vaccine Ontology ID: VO_0011446
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: F. tularensis chaperonin GroEL (Hsp60)
  • groEL gene engineering:
    • Type: Recombinant protein preparation
    • Description: Hsp60 was identified by Western blotting with a monoclonal antibody to GroEL (Sigma-Aldrich, Poole, United Kingdom). Hsp60 was excised from large-format unstained gels and electroeluted into 4× Laemmli buffer (0.1 M Tris-HCl [pH 7.3], 0.768 M glycine, 0.4% [wt/vol] SDS) by using the Hoefer gel eluter (Amersham Pharmacia, Buckinghamshire, United Kingdom) at 70 V for 2 h, following the manufacturer's instructions. The eluted product was pooled and purified by dilution (more than 20×) in ammonium bicarbonate (3.95 g/liter) and SDS (1 g/liter) and centrifuged over a dialysis membrane (10,000-molecular-weight cutoff; Vivascience, Lincoln, United Kingdom). The protein was then diluted (20×) in sterile water and centrifuged further, until significant concentration was achieved (Hartley et al., 2004).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intraperitoneal injection (i.p.)
References
Hartley et al., 2004: Hartley MG, Green M, Choules G, Rogers D, Rees DG, Newstead S, Sjostedt A, Titball RW. Protection afforded by heat shock protein 60 from Francisella tularensis is due to copurified lipopolysaccharide. Infection and immunity. 2004; 72(7); 4109-4113. [PubMed: 15213156].
H. influenzae Hap protein vaccine
Vaccine Information
  • Vaccine Name: H. influenzae Hap protein vaccine
  • Vaccine Ontology ID: VO_0011499
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: H. influenzae Hap
  • hap gene engineering:
    • Type: Recombinant protein preparation
    • Description: Bacteria were grown in 10 liters of BHI broth for 18 h at 35°C with aeration. All the following steps were performed at 4°C. Bacterial cells were removed by centrifugation at 10,000 × g. The culture supernatant was concentrated 20-fold by using an Amicon stir cell and was fractionated overnight with ammonium sulfate at 60% saturation. After centrifugation at 17,000 × g for 1 h, the precipitate was dissolved in 20 mM Tris buffer at pH 7.4 containing 50 mM NaCl and 1 mM EDTA, dialyzed against the same buffer, and then centrifuged at 100,000 × g for 1 h to remove insoluble material. The resulting supernatant was loaded at a flow rate of 2 ml/min onto a 20-ml SP Sepharose column (Amersham Pharmacia Biotech) equilibrated with the same buffer. The column was washed until the OD280 reached the baseline, and nHapS-P860295 was eluted at a flow rate of 3 ml/min with a linear gradient of NaCl (from 55 to 500 mM) in 20 mM Tris at pH 7.5 with 1 mM EDTA. Based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) gels, fractions containing nHapS-P860295 were pooled (Liu et al., 2004).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000143
    • Description: Mutant cholera toxin CT-E29H
  • Immunization Route: Subcutaneous injection
References
Liu et al., 2004: Liu DF, Mason KW, Mastri M, Pazirandeh M, Cutter D, Fink DL, St Geme JW 3rd, Zhu D, Green BA. The C-terminal fragment of the internal 110-kilodalton passenger domain of the Hap protein of nontypeable Haemophilus influenzae is a potential vaccine candidate. Infection and immunity. 2004 Dec; 72(12); 6961-8. [PubMed: 15557618].
H. influenzae Omp26 protein vaccine
Vaccine Information
  • Vaccine Name: H. influenzae Omp26 protein vaccine
  • Vaccine Ontology ID: VO_0011562
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: H. influenzae outer membrane protein 26
  • skp gene engineering:
    • Type: Recombinant protein preparation
    • Description: A crude outer membrane preparation was obtained from bacteria grown overnight on agar plates, and OMP26 was purified by preparative polyacrylamide gel electrophoresis (PAGE) as previously described. Preparative SDS-PAGE to purify OMP26 was performed with a Bio-Rad model 491 Prep Cell, using a 60-ml 14% T-1.42% C acrylamide-BIS (N,N′-methylenebisacrylamide) separating gel with a 10-ml 4% T-0.36% C acrylamide-BIS stacking gel polymerized in a 37-mm (internal diameter) column. Fractions were concentrated by lyophilization and analyzed for protein content by analytical SDS-PAGE. OMP26 isolated under these conditions contained SDS, which was subsequently removed. Fractions containing OMP26 were pooled and dialyzed prior to determination of protein concentration. The presence of lipooligosaccharide (LOS) was assessed by both silver staining of SDS-PAGE minigels and assaying with the E-TOXATE Limulus lysate test (Sigma, Castle Hill, New South Wales, Australia) (Kyd and Cripps, 1998).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Subserosal injection
References
Kyd and Cripps, 1998: Kyd JM, Cripps AW. Potential of a novel protein, OMP26, from nontypeable Haemophilus influenzae to enhance pulmonary clearance in a rat model. Infection and immunity. 1998; 66(5); 2272-2278. [PubMed: 9573117].
H. pylori catalase protein vaccine
Vaccine Information
  • Vaccine Name: H. pylori catalase protein vaccine
  • Vaccine Ontology ID: VO_0011513
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: H. pylori catalase
  • katA gene engineering:
    • Type: Recombinant protein preparation
    • Description: When required for use as a vaccine antigen, H. pylori was harvested from plates with 0.1 M phosphate-buffered saline (PBS), pelleted by centrifugation, and disrupted by sonication. The sonicate was stored at 220°C until use. Purified catalase was obtained by the method of Hazell et al. (11). Briefly, H. pylori cells were harvested with 0.1 M sodium phosphate buffer (pH 7.2), centrifuged, and then resuspended in the buffer. Cells were disrupted by sonication, cellular material was removed by centrifugation (5 min, 10,000 3 g), and then the supernatant was collected and filtered (0.22-mm-pore-size filter). Catalase was eluted by the creation of a gradient with 1 M NaCl in 0.01 M sodium phosphate buffer. The purified catalase was then filter sterilized, stored at 4°C, and protected from light (Radcliff et al., 1997).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
References
Radcliff et al., 1997: Radcliff FJ, Hazell SL, Kolesnikow T, Doidge C, Lee A. Catalase, a novel antigen for Helicobacter pylori vaccination. Infection and immunity. 1997; 65(11); 4668-4674. [PubMed: 9353048].
H. pylori GltA Protein Vaccine
Vaccine Information
  • Vaccine Name: H. pylori GltA Protein Vaccine
  • Vaccine Ontology ID: VO_0004062
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: Purified GltA protein
  • gltA gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: intra-Peyer's patch (IPP)
References
 
H. pylori HspA Protein Vaccine
Vaccine Information
  • Vaccine Name: H. pylori HspA Protein Vaccine
  • Vaccine Ontology ID: VO_0004060
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: Recombinant HspA protein
  • hspA gene engineering:
    • Type: Recombinant protein preparation
    • Description: The hspA gene was cloned into the expression vector pMAL-C2 and expressed in E. coli as a MalE fusion (Ferrero et al., 1995).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000143
    • Description: 5 μg of cholera toxin (Ferrero et al., 1995).
  • Immunization Route: Orally
References
Ferrero et al., 1995: Ferrero RL, Thiberge JM, Kansau I, Wuscher N, Huerre M, Labigne A. The GroES homolog of Helicobacter pylori confers protective immunity against mucosal infection in mice. Proceedings of the National Academy of Sciences of the United States of America. 1995; 92(14); 6499-6503. [PubMed: 7604021].
H. pylori HspB Protein Vaccine
Vaccine Information
  • Vaccine Name: H. pylori HspB Protein Vaccine
  • Vaccine Ontology ID: VO_0004061
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: Recombinant HspB protein
  • hspB gene engineering:
    • Type: Recombinant protein preparation
    • Description: The hspB gene was cloned into the expression vector pMAL-C2 and expressed in E. coli as a MalE fusion
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000143
    • Description: 5 μg of cholera toxin (Ferrero et al., 1995).
  • Immunization Route: Orally
References
 
H. pylori NAP protein vaccine
Vaccine Information
  • Vaccine Name: H. pylori NAP protein vaccine
  • Vaccine Ontology ID: VO_0011514
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: H. pylori neutrophil-activating protein
  • NAP gene engineering:
    • Type: Recombinant protein preparation
    • Description: HP-NAP was cloned and expressed in Bacillus subtilis to avoid contamination with LPS. Two preparations of HP-NAP were isolated from H. pylori CCUG strain (Satin et al., 2000).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intragastric
References
Satin et al., 2000: Satin B, Del Giudice G, Della Bianca V, Dusi S, Laudanna C, Tonello F, Kelleher D, Rappuoli R, Montecucco C, Rossi F. The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a protective antigen and a major virulence factor. The Journal of experimental medicine. 2000; 191(9); 1467-1476. [PubMed: 10790422].
H. pylori VacA protein vaccine
Vaccine Information
  • Vaccine Name: H. pylori VacA protein vaccine
  • Vaccine Ontology ID: VO_0011479
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: H. pylori vacuolating cytotoxin VacA
  • vacA gene engineering:
    • Type: Recombinant protein preparation
    • Description: VacA was purified from culture supernatant of H. pylori CCUG17874. Formaldehyde treatment was carried out by incubation of VacA (approximately 100 mg/ml) in a solution of phosphate-buffered saline (PBS) containing 25 mM lysine and 0.01% thimerosal (Sigma Chemicals, St. Louis, Mo.) plus different concentrations of formaldehyde for 48 h at 37°C followed by dialysis against PBS. Control VacA was treated in the same manner but in the absence of formaldehyde. VacA biological activity was assessed in a HeLa cell-vacuolating assay (14). Briefly, 104
      HeLa cells/well were seeded into 96-well flat-bottomed microtiter plates. After 16 h of incubation, the cells were treated for a further 8 h at 37°C with 2 mg of acid-activated VacA (2) in 100 ml of RPMI medium containing 2% fetal calf serum plus 5 mM ammonium chloride (Manetti et al., 1997).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Oral
References
Manetti et al., 1997: Manetti R, Massari P, Marchetti M, Magagnoli C, Nuti S, Lupetti P, Ghiara P, Rappuoli R, Telford JL. Detoxification of the Helicobacter pylori cytotoxin. Infection and immunity. 1997; 65(11); 4615-4619. [PubMed: 9353041].
Infanrix/Hib
Vaccine Information
  • Vaccine Name: Infanrix/Hib
  • Product Name: Combined diphtheria, tetanus, acellular pertussis (DTPa) and Haemophilus influenza type b vaccine
  • Tradename: Infanrix/Hib
  • Manufacturer: GlaxoSmithKline
  • Vaccine Ontology ID: VO_0010720
  • Type: Subunit vaccine
  • Status: Licensed
  • Location Licensed: Canada
  • Host Species for Licensed Use: Human
  • Adjuvant:
  • Preservative: 2 phenoxy ethanol
  • Allergen: Latex in plunger stopper of prefilled syringe
  • Immunization Route: Intramuscular injection (i.m.)
  • Storage: Refrigerated stored between +2°C and +8°C.
  • Approved Age for Licensed Use: 15 months and older
  • Description: Products: Proteins + conjugate. Other components: Formaldehyde, Lactose.
References
 
Infanrix/Hib
Vaccine Information
  • Vaccine Name: Infanrix/Hib
  • Product Name: Diphtheria-tetanus-acellular pertussis and Haemophilus influenzae type b (Hib) vaccine.
  • Tradename: Infanrix/Hib
  • Manufacturer: GlaxoSmithKline
  • Vaccine Ontology ID: VO_0010720
  • Type: Subunit vaccine
  • Status: Licensed
  • Location Licensed: Canada
  • Host Species for Licensed Use: Human
  • Adjuvant:
  • Preservative: 2 phenoxy ethanol
  • Allergen: Latex in plunger stopper of prefilled syringe
  • Immunization Route: Intramuscular injection (i.m.)
  • Storage: Store at 2°C – 8°C (in a refrigerator).
  • Approved Age for Licensed Use: 15 months and older
  • Description: Products: Proteins + conjugate. Other components: Formaldehyde, Lactose.
References
 
J5dLPS/OMP
Vaccine Information
  • Vaccine Name: J5dLPS/OMP
  • Vaccine Ontology ID: VO_0004201
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: Detoxified, O-polysaccharide side chain-deficient, lipopolysaccharide non-covalently complexed with the outer membrane protein of N. meningitidis group B (Gregory et al., 2010).
  • Adjuvant:
  • Immunization Route: intranasal immunization
References
Gregory et al., 2010: Gregory SH, Chen WH, Mott S, Palardy JE, Parejo NA, Heninger S, Anderson CA, Artenstein AW, Opal SM, Cross AS. Detoxified endotoxin vaccine (J5dLPS/OMP) protects mice against lethal respiratory challenge with Francisella tularensis SchuS4. Vaccine. 2010; 28(16); 2908-2915. [PubMed: 20170768].
M. gallisepticum TM-1 Protein Subunit Vaccine
Vaccine Information
References
 
Meningitec
Vaccine Information
  • Vaccine Name: Meningitec
  • Product Name: Meningococcal Group C Conjugate Vaccine (Diphtheria CRM197 Protein)
  • Tradename: Meningitec
  • Manufacturer: Berna Biotech, Wyeth Canada
  • Vaccine Ontology ID: VO_0010724
  • Type: Subunit vaccine
  • Status: Licensed
  • Location Licensed: Canada
  • Host Species for Licensed Use: Human
  • Adjuvant:
    • VO ID: VO_0000193
    • Description: Products: Conjugate.
  • Allergen: Latex in stopper of vial and plunger stopper of prefilled syringe
  • Immunization Route: Intramuscular injection (i.m.)
  • Storage: 2°C to 8°C (36°F to 46°F).
  • Approved Age for Licensed Use: 2 months of age and older.
  • Description: Products: Conjugate.
References
 
Microencapsulated Caf1 and LcrV vaccine
Vaccine Information
  • Vaccine Name: Microencapsulated Caf1 and LcrV vaccine
  • Vaccine Ontology ID: VO_0000837
  • Type: Subunit vaccine
  • Adjuvant:
    • VO ID: VO_0001241
    • Description: Current killed whole cell vaccines have been shown to cause a number of transient side effects, require frequent boosting to maintain immunity, and their efficacy against pneumonic infection is questionable. Thus, a new vaccine for plague based on the protective protein sub-units capsular Fraction 1 (Caf1) and LcrV is under development. The Caf1 molecule is a temperature-regulated capsular protein of Y. pestis which is maximally expressed at 37 °C and which has a role in resistance of phagocytosis. The LcrV antigen of Y. pestis is a 37 kDa secreted protein that is known to have a role in modulation of host defence mechanisms by down-regulating production of IFN-γ and TNF-α and and up-regulation of the anti-inflammatory cytokine IL-10. It is also believed to act as a virulence factor with a key role in the Type III secretion system of Y. pestis. Immunisation with recombinant LcrV antigen adsorbed to the adjuvant alhydrogel has been shown to confer protection against virulent challenge by both the sub-cutaneous and airborne routes. The use of the rCaf1 and rLcrV subunits in combination has been shown to have an additive effect on protection in murine models of infection and the two sub-units when formulated with alhydrogel are being taken forward into clinical trials as a vaccine for human use (Elvin et al., 2006)
  • Preparation: Recombinant Caf1 antigen was produced in Escherichia coli strain JM101 containing plasmid pAH34L, encoding the caf operon of Y. pestis strain GB. The rCaf1 was purified by ammonium sulfate fractionation followed by gel filtration chromatography. The LcrV antigen was expressed as a fusion protein with glutathione-S-transferase (GST) in E. coli using the plasmid pVG 110 for expression. The recombinant LcrV antigen was cleaved from the fusion protein with Factor Xa (Boehringer Mannheim UK Ltd.) and then purified by affinity chromatography. Microspheres were prepared using a modified solvent evaporation process. Freeze-dried rCaf1 or rLcrV (2 mg) was resuspended to form a PVA internal phase, which was then added to a polymer solution and sonicated on ice to form a water-in-oil primary emulsion. This was then added to PVA and homogenised to form a water-in-oil-in-water double emulsion. The microspheres were stirred overnight at room temperature to remove the solvent by the process of evaporation. Residual PVA and solvent were then removed by washing the microspheres. Briefly, the microspheres were centrifuged to form a pellet. The supernatant was removed and the pellet re-suspended in water twice. The final pellet was re-suspended in 2 ml water and freeze-dried. Microencapsulated rCaf1 was mixed with microencapsulated rLcrV and free antigen in solution was added to give a range of doses from 25 to 100 μg of each sub-unit (Elvin et al., 2006).
  • Virulence:
  • Description: Current killed whole cell vaccines have been shown to cause a number of transient side effects, require frequent boosting to maintain immunity, and their efficacy against pneumonic infection is questionable. Thus, a new vaccine for plague based on the protective protein sub-units capsular Fraction 1 (Caf1) and LcrV is under development. The Caf1 molecule is a temperature-regulated capsular protein of Y. pestis which is maximally expressed at 37 °C and which has a role in resistance of phagocytosis. The LcrV antigen of Y. pestis is a 37 kDa secreted protein that is known to have a role in modulation of host defence mechanisms by down-regulating production of IFN-γ and TNF-α and and up-regulation of the anti-inflammatory cytokine IL-10. It is also believed to act as a virulence factor with a key role in the Type III secretion system of Y. pestis. Immunisation with recombinant LcrV antigen adsorbed to the adjuvant alhydrogel has been shown to confer protection against virulent challenge by both the sub-cutaneous and airborne routes. The use of the rCaf1 and rLcrV subunits in combination has been shown to have an additive effect on protection in murine models of infection and the two sub-units when formulated with alhydrogel are being taken forward into clinical trials as a vaccine for human use (Elvin et al., 2006)
References
Elvin et al., 2006: Elvin SJ, Eyles JE, Howard KA, Ravichandran E, Somavarappu S, Alpar HO, Williamson ED. Protection against bubonic and pneumonic plague with a single dose microencapsulated sub-unit vaccine. Vaccine. 2006 May 15; 24(20); 4433-9. [PubMed: 16546306].
N. meningitidis ExbB Protein Vaccine
Vaccine Information
References
 
N. meningitidis LctP Protein Vaccine
Vaccine Information
References
 
N. meningitidis NspA Protein Vaccine
Vaccine Information
  • Vaccine Name: N. meningitidis NspA Protein Vaccine
  • Vaccine Ontology ID: VO_0004013
  • Type: Subunit vaccine
  • Status: Research
  • NspA from N. meningitidis MC58 gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0001263
    • Description: QuilA (CedarLane Laboratories, Hornby, Ontario, Canada) (Martin et al., 1997).
  • Immunization Route: Intraperitoneal injection (i.p.)
References
 
N. meningitidis TbpA Protein Vaccine
Vaccine Information
  • Vaccine Name: N. meningitidis TbpA Protein Vaccine
  • Vaccine Ontology ID: VO_0004064
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: rTbpA
  • tbpA gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000139
    • Description: Vaccines were prepared with an equal volume of either Freund's complete adjuvant (first immunization) or Freund's incomplete adjuvant (subsequent immunizations) (West et al., 2001).
  • Adjuvant:
    • VO ID: VO_0000142
    • Description: Vaccines were prepared with an equal volume of either Freund's complete adjuvant (first immunization) or Freund's incomplete adjuvant (subsequent immunizations) (West et al., 2001).
  • Immunization Route: subcutaneous injection
References
 
N. miningitidis TBP2 Protein Vaccine
Vaccine Information
References
 
Non-typeable H. influenzae rLP4/rLP6 and Moraxella catarrhalis UspA2 protein vaccine
Vaccine Information
  • Vaccine Name: Non-typeable H. influenzae rLP4/rLP6 and Moraxella catarrhalis UspA2 protein vaccine
  • Vaccine Ontology ID: VO_0000473
  • Type: Subunit vaccine
  • Antigen: NTHi rLP4/rLP6 and M. catarrhalis UspA2 proteins(Mason et al., 2004)
  • Pal gene engineering:
    • Type: recombinant
    • Description: The P6 protein is an integral outer membrane protein and, as a peptidoglycan-associated lipoprotein , is thought to be necessary for the integrity of the bacterium’s outer membrane.(Mason et al., 2004)
    • Detailed Gene Information: Click Here.
  • yscF gene engineering:
    • Type: recombinant
    • Description: The P4 protein is an integral outer membrane protein that has a role in acquiring hemin and nucleosides.(Green et al., 1991)
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Preparation: Recombinant nontypeable H. influenzae LP4 (rLP4) and LP6 (rLP6) were expressed in E. coli strain BLR and purified (Mason et al., 2004). M. catarrhalis UspA was purified from outer membrane vesicles prepared from isolate O35E (Mason et al., 2004).
  • Description: Nontypeable Haemophilus influenzae (NTHi) and Moraxella catarrhalis are two of the leading causes of bacterial otitis media. The immunodominant exposed surface molecules of NTHi, including lipooligosaccharide (LOS) and outer membrane proteins, are extremely variable antigenically and infection with one strain provides immunity only to that strain. Thus, NTHi vaccine efforts have focused on antigenically conserved outer membrane protein such as the P4 and P6 proteins and LOS-conjugates. While the surface of M. catarrhalis appears to be much less antigenically variable, vaccine efforts have also focused on conserved outer membrane proteins and LOS. The ubiquitous cell surface protein A (UspA) of M. catarrhalis is a particularly interesting vaccine candidate (Mason et al., 2004).
References
Mason et al., 2004: Mason KW, Zhu D, Scheuer CA, McMichael JC, Zlotnick GW, Green BA. Reduction of nasal colonization of nontypeable Haemophilus influenzae following intranasal immunization with rLP4/rLP6/UspA2 proteins combined with aqueous formulation of RC529. Vaccine. 2004 Sep 3; 22(25-26); 3449-56. [PubMed: 15308371].
Nontypeable H. influenzae cell membrane (CM-Hi) vaccine
Vaccine Information
  • Vaccine Name: Nontypeable H. influenzae cell membrane (CM-Hi) vaccine
  • Vaccine Ontology ID: VO_0000479
  • Type: Subunit vaccine
  • Antigen: Nontypeable Haemophilus influenzae cell membrane
  • Adjuvant:
  • Preparation: NTHi (strain 76), which was isolated from the nasopharynx of a patient with OME at Oita Medical University, was stored at -80°C and used for the preparation of antigen and nasal inoculation. NTHi was cultured overnight on chocolate agar and harvested by being scraped from the plate, suspended in EDTA buffer (pH 7.4). The bacterial cells were then disrupted by sonication on ice, and the unbroken cells and debris were removed by centrifugation at 10,000 g for 20 min. The supernatants were pooled and centrifuged at 80,000 g for 2 h at 4°C. The clear, gel-like pellet was suspended in distilled water and lyophilized. The resulting powder, referred to as cell membrane preparation from NTHi (CM-Hi), was stored until used in the experiments (Kurono et al., 1999).
References
Kurono et al., 1999: Kurono Y, Yamamoto M, Fujihashi K, Kodama S, Suzuki M, Mogi G, McGhee JR, Kiyono H. Nasal immunization induces Haemophilus influenzae-specific Th1 and Th2 responses with mucosal IgA and systemic IgG antibodies for protective immunity. The Journal of infectious diseases. 1999 Jul; 180(1); 122-32. [PubMed: 10353870].
Nontypeable H. influenzae Hap Protein Vaccine
Vaccine Information
  • Vaccine Name: Nontypeable H. influenzae Hap Protein Vaccine
  • Vaccine Ontology ID: VO_0000432
  • Type: Subunit vaccine
  • Antigen: Recombinant proteins corresponding to the C-terminal region of HapS from H. influenzae strains N187, P860295, and TN106.
  • hap gene engineering:
    • Type: recombinant
    • Detailed Gene Information: Click Here.
  • hap gene engineering:
    • Type: recombinant
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000143
    • Description: CT-E29H (a mutant cholera toxin)
  • Preparation: Recombinant proteins corresponding to the C-terminal region of HapS from H. influenzae strains N187, P860295, and TN106 were used. To prepare the protein antigens for vaccination, 15 µg of rCBD was diluted in Dulbecco's PBS (D-PBS) to a final volume of 20 to 40 µl with or without 0.1 µg of CT-E29H (a mutant cholera toxin) as an adjuvant (Liu et al., 2004).
  • Description: Nontypeable Haemophilus influenzae (NTHi), a nonencapsulated gram-negative bacterium, is the cause of a number of human respiratory tract diseases, such as otitis media, sinusitis, bronchitis, and pneumonia. Hap adhesin, promotes bacterial interaction with human respiratory epithelial cells and extracellular matrix proteins as well as mediates bacterial aggregation and microcolony formation. Hap belongs to the autotransporter family of proteins common among gram-negative pathogens . It is synthesized as a 155-kDa precursor protein, which consists of an N-terminal 25-amino-acid signal peptide, an internal 110-kDa passenger domain called HapS, and a C-terminal 45-kDa outer membrane domain called Hapß. Domain in Hap responsible for promoting adherence to epithelial cells resides in the C-terminal 311 amino acids the (cell binding domain [CBD]) of HapS (Liu et al., 2004).
References
Liu et al., 2004: Liu DF, Mason KW, Mastri M, Pazirandeh M, Cutter D, Fink DL, St Geme JW 3rd, Zhu D, Green BA. The C-terminal fragment of the internal 110-kilodalton passenger domain of the Hap protein of nontypeable Haemophilus influenzae is a potential vaccine candidate. Infection and immunity. 2004 Dec; 72(12); 6961-8. [PubMed: 15557618].
Nontypeable H. influenzae NucA Protein vaccine
Vaccine Information
  • Vaccine Name: Nontypeable H. influenzae NucA Protein vaccine
  • Vaccine Ontology ID: VO_0004038
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: NucA Protein
  • nucA gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0001250
    • Description: MPL (3-O-deacylated monophosphoryl lipid A.
  • Preparation: The native protein was extracted from NTHi strain P860295 with KSCN and purified. The recombinant protein was cloned, sequenced, and expressed in Escherichia coli. The recombinant protein is localized in the periplasm of E. coli and has been purified to homogeneity. Both the recombinant and native proteins possess 5'-nucleotidase activity (Zagursky et al., 2000).
  • Immunization Route: Intraperitoneal injection (i.p.)
  • Description: A surface-exposed, highly conserved, immunogenic NTHi protein was identified, which elicits cross-reactive bactericidal antibodies against NTHi (Zagursky et al., 2000). This protein, called NucA, has been identified as a 5' nucleotidase and has been cloned, sequenced, and expressed recombinantly. It elicits broadly cross-reactive antibody against NTHi strains and has vaccine potential.
References
Zagursky et al., 2000: Zagursky RJ, Ooi P, Jones KF, Fiske MJ, Smith RP, Green BA. Identification of a Haemophilus influenzae 5'-nucleotidase protein: cloning of the nucA gene and immunogenicity and characterization of the NucA protein. Infection and immunity. 2000 May; 68(5); 2525-34. [PubMed: 10768940].
Nontypeable H. influenzae Outer Membrane Protein P1 vaccine
Vaccine Information
  • Vaccine Name: Nontypeable H. influenzae Outer Membrane Protein P1 vaccine
  • Vaccine Ontology ID: VO_0004110
  • Type: Subunit vaccine
  • Antigen: Outer Membrane Protein P1
  • ompP1 gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Preparation: OmpP1 was cloned from the clinical NTHI strain BCH-3 and expressed P1 in the cytoplasm of E. coli (rP1BCH-3 ).
  • Description: OMP P1 (47 kDa) accounts for ~10% of H. influenzae OMP content. Passive immunization with P1 induces protection against bacteremia in the infant rat model. OMP P1 has eight potentially surface-exposed loops, four of which are immunogenic. The availability of several ompP1 sequences was particularly relevant, as it offered the information needed for a broader survey of the sequence conservation of the ompP1 gene across a phylogenically classified collection of >500 typeable H. influenzae and NTHI isolates representing the natural population structure of the species (Bolduc et al., 2000).
References
Bolduc et al., 2000: Bolduc GR, Bouchet V, Jiang RZ, Geisselsoder J, Truong-Bolduc QC, Rice PA, Pelton SI, Goldstein R. Variability of outer membrane protein P1 and its evaluation as a vaccine candidate against experimental otitis media due to nontypeable Haemophilus influenzae: an unambiguous, multifaceted approach. Infection and immunity. 2000 Aug; 68(8); 4505-17. [PubMed: 10899849].
Nontypeable H. influenzae outer membrane recombinant P4 vaccine
Vaccine Information
  • Vaccine Name: Nontypeable H. influenzae outer membrane recombinant P4 vaccine
  • Vaccine Ontology ID: VO_0004114
  • Type: Subunit vaccine
  • Antigen: Recombinant lipidated P4 and the non-fatty acylated recombinant P6 protein that contains a 7-amino acid peptide genetically fused to the N-terminus (rP6) were used as vaccine candidates (Hotomi et al., 2005).
  • Adjuvant:
  • Preparation: The lipidated form of recombinant P4 protein (rP4) was expressed in E. coli strain BLR (Novagen, Madison, WI) transformed with plasmid pLP339. Plasmid pLP339 contains the wild type P4 gene cloned into the multiple cloning sites of pBAD18 cm (Invitrogen Corp., Carlsbad, CA) under control of the arabinose promoter. The non-fatty acylated recombinant P6 protein (rP6) was expressed in plasmid pRSM1007 in E coli strain BL21(DE3). Plasmid pRSM1007 contain A P6 DNA fragment encoding the mature protein devoid of lipidation signal sequence was amplified from Hib strain MinnA chromosomal DNA (Hotomi et al., 2005).
References
Hotomi et al., 2005: Hotomi M, Ikeda Y, Suzumoto M, Yamauchi K, Green BA, Zlotnick G, Billal DS, Shimada J, Fujihara K, Yamanaka N. A recombinant P4 protein of Haemophilus influenzae induces specific immune responses biologically active against nasopharyngeal colonization in mice after intranasal immunization. Vaccine. 2005 Jan 26; 23(10); 1294-300. [PubMed: 15652672].
nontypeable H. influenzae P5 peptide MVF/H3 vaccine
Vaccine Information
  • Vaccine Name: nontypeable H. influenzae P5 peptide MVF/H3 vaccine
  • Vaccine Ontology ID: VO_0000509
  • Type: Subunit vaccine
  • Antigen: Peptides representing conserved regions of the NTHi P5 outer membrane protein which have been fused to a promiscuous measles virus F protein T-cell eptitope (MVF) (Webb et al., 2000).
  • Adjuvant:
  • Preparation: The sequences of the peptides were based on the sequence of P5 from NTHi strain UC19. Peptide L1A encompasses the amino acid motif GINNNGAIK, which is found in loop one in a subset of NTHi strains, including UC19; L4 encompasses the highly conserved central region of loop four; and H3 encompasses a region in P5 that is homologous to OprF peptide 10 from P. aeruginosa .The peptides also contained the measles virus F protein promiscuous T-cell epitope (MVF) and a linker region composed of a 4-residue (LSPG) beta -turn. Peptides were synthesized and purified and by the Biomolecular Resource Facility (Webb et al., 2000) .
References
Webb et al., 2000: Webb DC, Cripps AW. A P5 peptide that is homologous to peptide 10 of OprF from Pseudomonas aeruginosa enhances clearance of nontypeable Haemophilus influenzae from acutely infected rat lung in the absence of detectable peptide-specific antibody. Infection and immunity. 2000 Jan; 68(1); 377-81. [PubMed: 10603411].
Nontypeable H. influenzae protein P6 with cholera toxin
Vaccine Information
  • Vaccine Name: Nontypeable H. influenzae protein P6 with cholera toxin
  • Vaccine Ontology ID: VO_0000614
  • Type: Subunit vaccine
  • Antigen: outer membrane protein P6 (Sabirov et al., 2004)
  • Adjuvant:
  • Preparation: NTHI was grown on chocolate agar plates and suspended in phosphate-buffered saline (PBS). The suspension was sonicated and centrifuged at 21,000 × g for 30 min at room temperature. The pellet was resuspended in 1% sodium dodecyl sulfate with 0.1 M Tris, 0.5 M NaCl, and 0.1% 2-mercaptoethanol (buffer B, pH 8.0) with RNase (10 mg/ml), sonicated, incubated, and centrifuged. This procedure was repeated twice. The pellet was then suspended in buffer B without RNase, sonicated, incubated, and centrifuged again. The pellet was finally suspended in buffer A (0.01 M Tris, 0.15 M NaCl; pH 7.4) and incubated at 65°C for 30 min. The insoluble material was removed by centrifugation at 100,000 × g for 60 min at 30°C. The protein contained in the supernatant was thought to be pure P6 (Sabirov et al., 2004).
References
Sabirov et al., 2004: Sabirov A, Kodama S, Sabirova N, Mogi G, Suzuki M. Intranasal immunization with outer membrane protein P6 and cholera toxin induces specific sinus mucosal immunity and enhances sinus clearance of nontypeable Haemophilus influenzae. Vaccine. 2004 Aug 13; 22(23-24); 3112-21. [PubMed: 15297063].
Nontypeable H. influenzae rTbpB vaccine
Vaccine Information
  • Vaccine Name: Nontypeable H. influenzae rTbpB vaccine
  • Vaccine Ontology ID: VO_0000510
  • Type: Subunit vaccine
  • Antigen: Nontypeable H. influenzae vaccine recombinant transferrin binding protein B
  • Adjuvant:
  • Preparation: The NTHI strain UC19 (289-I) was originally derived from the sputum of a patient with chronic bronchitis and has been routinely used in this laboratory as the challenge strain when assessing the efficacy of immunization with NTHI antigens. The gene encoding the mature form of UC19 TbpB was then amplified and cloned into the BamHI restriction sites in plasmid pGEX2T (Pharmacia Biotech, Uppsala, Sweden) to produce plasmid pCU17. This plasmid is engineered to express recombinant TbpB as a glutathione S-transferase (GST) fusion protein with a thrombin cleavage recognition site between the two proteins (Webb et al., 1999).
  • Description: The transferrin receptor is composed of two subunits. The interaction of the receptor with transferrin is probably initiated by transferrin binding protein B (TbpB), a peripheral lipoprotein that forms a complex with TbpA, a TonB-dependent integral outer membrane protein that is thought to form a gated pore to facilitate the transport of transferrin-derived iron across the outer membrane (Webb et al., 1999).
References
Webb et al., 1999: Webb DC, Cripps AW. Immunization with recombinant transferrin binding protein B enhances clearance of nontypeable Haemophilus influenzae from the rat lung. Infection and immunity. 1999 May; 67(5); 2138-44. [PubMed: 10225866].
P. aeruginosa OprI Protein Vaccine
Vaccine Information
  • Vaccine Name: P. aeruginosa OprI Protein Vaccine
  • Vaccine Ontology ID: VO_0004190
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: Recombinant OprI protein
  • OprI gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000127
    • Description: 100 μl of 1.5% Al(OH)3 (Finke et al., 1990).
  • Immunization Route: Intraperitoneal injection (i.p.)
References
 
P. aeruginosa PcrV Protein Vaccine
Vaccine Information
  • Vaccine Name: P. aeruginosa PcrV Protein Vaccine
  • Vaccine Ontology ID: VO_0004191
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: PcrV
  • PcrV gene engineering:
    • Type: Recombinant protein preparation
    • Description: PcrV was produced as a lipopolysaccharide-free histidine-tagged infusion protein in pET16b and was purified by nickel chromatography (Holder et al., 2001).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000142
    • Description: 0.1 ml of incomplete Freund's adjuvant (Holder et al., 2001).
  • Immunization Route: Intramuscular injection (i.m.)
References
Holder et al., 2001: Holder IA, Neely AN, Frank DW. PcrV immunization enhances survival of burned Pseudomonas aeruginosa-infected mice. Infection and immunity. 2001; 69(9); 5908-5910. [PubMed: 11500471].
P1-HspB (fusion of protein 1 and heat-shock protein B)
Vaccine Information
  • Vaccine Name: P1-HspB (fusion of protein 1 and heat-shock protein B)
  • Vaccine Ontology ID: VO_0004133
  • Type: Subunit vaccine
  • p1 gene engineering:
    • Type: Recombinant protein preparation
    • Description: The primers were synthesized and the target DNA fragments were amplified by PCR from C. burnetii genomic DNA. The mixture used during amplification consisted of 0.3 M primer, 200 M deoxynucleoside triphosphate, and 0.6 U of Taq polymerase (Li et al., 2005). See preparation below for more information.
    • Detailed Gene Information: Click Here.
  • htpB gene engineering:
    • Type: Recombinant protein preparation
    • Description: The primers were synthesized and the target DNA fragments were amplified by PCR from C. burnetii genomic DNA. The mixture used during amplification consisted of 0.3 M primer, 200 M deoxynucleoside triphosphate, and 0.6 U of Taq polymerase (Li et al., 2005). See preparation below for more information.
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Adjuvant:
  • Preparation: Gene fragments encoding C. burnetii outer membrane protein 1 (P1) and heat-shock protein B (HspB) are amplified by PCR from genomic DNA extracted from C. burnetii. The amplified p1 and hspB gene fragments are purified and digested with DNA endonuclease pairs BamHI/ScaI and SacI/PstI, respectively. The genes are then ligated with pQE30 (digested with homologous enzyme pair) with T4 ligase, resulting in recombinant expression plasmids pQE30/p1 and pQE30/hspB. Plasmid pQE30/p1-hspB is constructed by ligating hspB of pQE30/hspB with p1 fragment from pQE30/p1. E.coli M15 cells are then transformed with the ligation mixtures and screened on medium containing ampicillin and kanamycin. The E. coli cells were propagated in LB medium and induced by IPTG. The resulting recombinant proteins were purified by affinity chromatography with nickel-nitrilotriacetic resin (Li et al., 2005).
References
Li et al., 2005: Li Q, Niu D, Wen B, Chen M, Qiu L, Zhang J. Protective immunity against Q fever induced with a recombinant P1 antigen fused with HspB of Coxiella burnetii. Annals of the New York Academy of Sciences. 2005; 1063; 130-142. [PubMed: 16481504 ].
Porin and S-LPS Extracted from Virulent Brucella abortus 2308
Vaccine Information
  • Vaccine Name: Porin and S-LPS Extracted from Virulent Brucella abortus 2308
  • Vaccine Ontology ID: VO_0000403
  • Type: Subunit vaccine
  • Antigen: The antigen for this vaccine is a complex of porin and smooth lipopolysaccharide (S-LPS) extracted from virulent Brucella abortus 2308 (Winter et al., 1988).
  • Adjuvant:
    • VO ID: VO_0001250
    • Description: The porin-S-LPS was given without adjuvant or in several adjuvants: trehalose dimycolate and muramyl dipeptide; the pluronic polymer L-121 and muramyl dipeptide; or complexed with Quil A in immunostimulating complexes (Winter et al., 1988).
  • Preparation: The S-LPS was produced from smooth strain 2308 by extraction in hot phenol followed by treatment with guanidinium thiocyanate. Inocula were prepared from a freshly thawed vial which was diluted in sterile phosphate buffered saline to yield an infecting dose of 5 x 10^4 bacteria per 0.1 ml. Each dose was mixed with its appropriate adjuvant (Winter et al., 1988).
References
Winter et al., 1988: Winter AJ, Rowe GE, Duncan JR, Eis MJ, Widom J, Ganem B, Morein B. Effectiveness of natural and synthetic complexes of porin and O polysaccharide as vaccines against Brucella abortus in mice. Infection and immunity. 1988; 56(11); 2808-2817. [PubMed: 2844673].
Recombinant Brucella DnaK protein vaccine
Vaccine Information
  • Vaccine Name: Recombinant Brucella DnaK protein vaccine
  • Vaccine Ontology ID: VO_0000373
  • Type: Subunit vaccine
  • Antigen: The antigen for this vaccine is rDnaK protein from B. abortus strain 2308, B. abortus strain S19, and Brucella melitensis strain H38 (Delpino et al., 2007).
  • Adjuvant:
    • VO ID: VO_0000139
    • Description: Two different adjuvants were used in these vaccines: Complete Freund's Adjuvant (CFA) and Incomplete Freund's Adjuvant (IFA). CFA was administered on day 0 and IFA was administered on day 15 (Delpino et al., 2007).
  • Adjuvant:
    • VO ID: VO_0000142
    • Description: Two different adjuvants were used in these vaccines: Complete Freund's Adjuvant (CFA) and Incomplete Freund's Adjuvant (IFA). CFA was administered on day 0 and IFA was administered on day 15 (Delpino et al., 2007).
  • Preparation: The open reading frame of DnaK was cloned in the Pet17b vector (Novagen, Madison, WI, USA). The specific primers for B. abortus DnaK contain with XbaI and BamHI restriction sites at the 5′ ends: sense 5′ GCAGTTTCTAGAATGGAGAGAAATA 3′, antisense 5′ TAAAAGGATCCAATTACGACGAC 3′. B. abortus genomic DNA was used as template for PCR with Pfu DNA polymerase (Stratagene). Plasmid Pet17b was digested with BamHI and NheI. After ligation, the mix was used to transform E. coli JM109 competent cells. The plasmid DNA of a clone containing the insert was purified and used to transform E. coli strain BL21 (DE3) competent cells. Upon induction with 1 mM isopropyl-β-d-thiogalactopyranoside (IPTG), recombinant DnaK (rDnaK) was successfully expressed, and purified using a Mono Q column in an AKTA apparatus (Amersham Pharmacia, Uppsala, Sweden). Recombinant proteins were adsorbed with Sepharose-polymyxin B (Sigma, St. Louis, MO) to eliminate lipopolysaccharide contamination (Delpino et al., 2007).
References
Delpino et al., 2007b: Delpino MV, Estein SM, Fossati CA, Baldi PC, Cassataro J. Vaccination with Brucella recombinant DnaK and SurA proteins induces protection against Brucella abortus infection in BALB/c mice. Vaccine. 2007; 25(37-38); 6721-6729. [PubMed: 17686554].
recombinant nontypeable H. influenzae protein P6 with AdDP
Vaccine Information
  • Vaccine Name: recombinant nontypeable H. influenzae protein P6 with AdDP
  • Vaccine Ontology ID: VO_0000558
  • Type: Subunit vaccine
  • Antigen: outer membrane protein P6
  • Pal gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Preparation: A DNA fragment encoding the mature P6 protein was amplified from the H. influenzae type a chromosomal DNA by use of PCR. The resulting PCR product was purified, digested with BamHI and SalI, ligated into the vector pCR2.1-TOPO (TOPO TA Cloning; Invitrogen), and then transformed into the E. coli strain XL-1 blue. The fragment encompassing the P6 gene was subsequently cloned into the expression vector pET23a+ (Novagen) and was transformed into E. coli BL21 (DE3) strain.The purity and identity of the purified rP6 protein was verified by SDS-PAGE and Western blot analysis, respectively, by use of mice antiserum raised against native P6 protein (Bertot et al., 2004).
References
Bertot et al., 2004: Bertot GM, Becker PD, Guzman CA, Grinstein S. Intranasal vaccination with recombinant P6 protein and adamantylamide dipeptide as mucosal adjuvant confers efficient protection against otitis media and lung infection by nontypeable Haemophilus influenzae. The Journal of infectious diseases. 2004 Apr 1; 189(7); 1304-12. [PubMed: 15031801].
Recombinant Y. pestis V antigen vaccine
Vaccine Information
  • Vaccine Name: Recombinant Y. pestis V antigen vaccine
  • Vaccine Ontology ID: VO_0000831
  • Type: Subunit vaccine
  • LcrV from Y. pestis biovar Microtus str. 91001 gene engineering:
    • Type: Protein
    • Detailed Gene Information: Click Here.
  • LcrV from Y. pestis KIM 10 gene engineering:
    • Type: Protein
    • Description: Protein coding
    • Detailed Gene Information: Click Here.
  • LcrV from y. pestis CO92 gene engineering:
    • Type: Protein
    • Description: Protein coding; V antigen; low calcium response protein V; functions in needle complex protein export; Yop secretion and targeting control protein; important for translocation pore formation; induces IL-10 production by macrophages; interacts with Toll-like receptor 2.
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Preparation: The gene encoding V antigen (lcrV) was amplified from Y. pestis DNA by PCR. The fragment was purified, digested with EcoRI and SalI, ligated with suitably digested plasmid pGEX-5X-2, and transformed into E. coli JM109 by electroporation. One-milliliter aliquots were removed from the cultures in the logarithmic and stationary phases, and the number of viable cells was determined by inoculating the aliquots onto L agar containing 100 mg of ampicillin/ml. The cells were harvested from a second 1-ml aliquot by centrifugation and resuspended in 1 ml of phosphate-buffered saline (PBS). The cell suspension was frozen at 2208C for 1 h, thawed, and then sonicated on ice at 10% power three times for 30 s each. The sonicates and a standard solution of rV (5 mg/ml) were serially diluted in PBS in a microtiter plate and allowed to bind overnight. The GST-V fusion protein was eluted with 10 ml of 50 mM Tris containing 5 mM reduced glutathione. After dialysis against PBS, the fusion protein was cleaved with factor Xa at an enzyme/fusion protein ratio of approximately 1:200 by weight. Cleaved GST and excess uncleaved GST-V (but not factor Xa) were removed from the solution by affinity adsorption to leave purified rV (Leary et al., 1995). Other recombinant V antigen (rV) expression systems, besides the N-terminal GST fusion pGEX-5X-2, include the pGEX-6P-2 systems from Pharmacia Biotech and the C-terminal CBD fusion (IMPACT I) system from New England Biolabs (Carr et al., 1999).
  • Virulence:
References
Carr et al., 1999: Carr S, Miller J, Leary SE, Bennett AM, Ho A, Williamson ED. Expression of a recombinant form of the V antigen of Yersinia pestis, using three different expression systems. Vaccine. 1999 Aug 20; 18(1-2); 153-9. [PubMed: 10501245].
Leary et al., 1995: Leary SE, Williamson ED, Griffin KF, Russell P, Eley SM, Titball RW. Active immunization with recombinant V antigen from Yersinia pestis protects mice against plague. Infection and immunity. 1995 Aug; 63(8); 2854-8. [PubMed: 7622205].
Recombinant Y. pestis YopD protein vaccine
Vaccine Information
  • Vaccine Name: Recombinant Y. pestis YopD protein vaccine
  • Vaccine Ontology ID: VO_0000834
  • Type: Subunit vaccine
  • LcrV from Y. pestis CO92 gene engineering:
    • Type: Protein
    • Detailed Gene Information: Click Here.
  • YopD from Y. pestis CO92 gene engineering:
    • Type: Protein
    • Description: Yop targeting negative regulator; translocon component; important for translocation pore formation.
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Preparation: The yopD loci from Yersinia pestis was amplified by PCR, cloned, and expressed in Escherichia coli. The purified protein was mixed with an equal volume of the adjuvant to give a final protein concentration of 100 µg/ml (Andrews et al., 1999).
  • Virulence:
  • Description: Yersinia outer proteins (Yops) are virulence determinants synthesized by the Yersinia species pathogenic for humans, including Y. pestis, the causative agent of plague. The Yop proteins are encoded on a 75-kb plasmid, and in vitro expression from these genes, as well as subsequent secretion and translocation by a Type III secretion system, are regulated by temperature, calcium, and eukaryotic cell contact. There are various functions known for some of the Yops, including translocation and sensor functions in Yop B/D and Yop N. Previous studies showed that antibodies to some Yops are present in convalescent-phase serum from patients infected with Y. pestis, as well as in rodent serum after experimental Y. pestis infection, which suggests that Yops are antigenic. Vaccination with Yop-containing culture supernatants from growth-restricted Yersinia enterocolitica protected mice from a lethal intraperitoneal (i.p.) dose of virulent Y. pestis; however, interpretation is complicated by the likely presence of V antigen in the crude supernatants, as V is known to be a protective antigen (Andrews et al., 1999).
References
Andrews et al., 1999: Andrews GP, Strachan ST, Benner GE, Sample AK, Anderson GW Jr, Adamovicz JJ, Welkos SL, Pullen JK, Friedlander AM. Protective efficacy of recombinant Yersinia outer proteins against bubonic plague caused by encapsulated and nonencapsulated Yersinia pestis. Infection and immunity. 1999 Mar; 67(3); 1533-7. [PubMed: 10024607 ].
Recombinant Yersinia rV10 vaccine
Vaccine Information
  • Vaccine Name: Recombinant Yersinia rV10 vaccine
  • Vaccine Ontology ID: VO_0000840
  • Type: Subunit vaccine
  • Adjuvant:
    • VO ID: VO_0001241
    • Description: Immunization with purified recombinant LcrV (rLcrV) is sufficient to generate protective immunity to both bubonic plague and pneumonic plague in mice, guinea pigs, and non-human primates. LcrV injection of animals triggered release of interleukin-10, a cytokine that suppresses innate immune functions. LcrV also prevents the release of proinflammatory cytokines (gamma interferon and tumor necrosis factor ) in murine and human macrophages. Considering the immune modulatory properties of rLcrV, there are concerns regarding the safety of LcrV vaccines in humans. Thus, there is an emphasis upon searching for variants with reduced immune modulatory properties. rV10, a variant lacking amino acids 271 to 300 of LcrV, displayed a significant decrease in its ability to induce interleukin-10 and to suppress tumor necrosis factor or gamma interferon release (DeBord et al., 2006).
  • Preparation: Escherichia coli BL21(DE3) carrying prV10 was grown overnight at 37 °C in Luria-Bertani medium (Difco) with 100 µg/ml ampicillin. Bacteria were diluted in fresh medium and grown to an optical density at 600 nm of 0.8 to 1.0. T7 polymerase expression was induced with 1 mM isopropyl-ß-D-thiogalactopyranoside, and bacterial growth was continued for 3 hours at 37°C. Cells were harvested by centrifugation at 10,000 x g for 10 min. Bacterial sediment was suspended in 20 ml of Tris-HCl (pH 7.5)-150 mM NaCl (column buffer) containing 100 µM phenylmethylsulfonyl fluoride, and cells were disrupted by two passages through a French pressure cell at 14,000 lb/in2. The lysate was subjected to ultracentrifugation at 40,000 x g for 30 min, and the soluble fraction was applied to a nickel nitrilotriacetic acid column (1-ml bed volume) preequilibrated with 10 ml of column buffer. The column was washed with 10 ml of the same buffer, followed by a second (10 ml of column buffer with 10% glycerol) and a third (10 ml of column buffer with 10% glycerol and 20 mM imidazole) washing. Bound protein was eluted in 50 mM Tris-HCl (pH 7.5), 150 mM NaCl, and 10% glycerol containing 250 mM imidazole. Purified proteins were subjected to three sequential Triton X-114 (Sigma) phase separations to remove endotoxins. Purified proteins were applied to a G-25 (Amersham) gel filtration column to remove residual Triton X-114 and then retrieved by phosphate-buffered saline elution. Lipopolysaccharide contamination of purified proteins was assayed with Limulus amebocyte lysate (QCL-1000; Cambrex, New Jersey) and determined to be less than 1 ng/100 µg of purified protein. Protein concentrations were determined by the bicinchoninic acid assay (Pierce Technology, Rockford, IL). Proteins were aliquoted at 1 mg/ml and stored at –80 °C for further use. Purified recombinant rV10 vaccine antigens were emulsified with Alhydrogel (DeBord et al., 2006).
  • Virulence:
  • Description: Immunization with purified recombinant LcrV (rLcrV) is sufficient to generate protective immunity to both bubonic plague and pneumonic plague in mice, guinea pigs, and non-human primates. LcrV injection of animals triggered release of interleukin-10, a cytokine that suppresses innate immune functions. LcrV also prevents the release of proinflammatory cytokines (gamma interferon and tumor necrosis factor ) in murine and human macrophages. Considering the immune modulatory properties of rLcrV, there are concerns regarding the safety of LcrV vaccines in humans. Thus, there is an emphasis upon searching for variants with reduced immune modulatory properties. rV10, a variant lacking amino acids 271 to 300 of LcrV, displayed a significant decrease in its ability to induce interleukin-10 and to suppress tumor necrosis factor or gamma interferon release (DeBord et al., 2006).
References
DeBord et al., 2006: DeBord KL, Anderson DM, Marketon MM, Overheim KA, DePaolo RW, Ciletti NA, Jabri B, Schneewind O. Immunogenicity and protective immunity against bubonic plague and pneumonic plague by immunization of mice with the recombinant V10 antigen, a variant of LcrV. Infection and immunity. 2006 Aug; 74(8); 4910-4. [PubMed: 16861680].
rF1 + rV
Vaccine Information
  • Vaccine Name: rF1 + rV
  • Vaccine Ontology ID: VO_0000830
  • Type: Subunit vaccine
  • Adjuvant:
    • VO ID: VO_0001241
    • Description: This vaccine utilizes a combination of the Fraction 1 antigen (F1) and the V antigen of Y. pestis in an optimum molar ratio. The F1 and V antigens, in recombinant form in this vaccine, are natural virulence factors of Y. pestis. Fraction 1 antigen, the major protein component of the capsule surrounding Y. pestis cells, is expressed only at 37 °C and it is believed to have anti-phagocytic activity. High anti-F1 titres have been correlated with survival following plague infection. Recombinant F1 antigen (rF1) has been produced by cloning the caf operon from Y. pestis into Escherichia coli and the protection provided by highly purified native F1 and recombinant F1 against Y. pestis has been demonstrated not to differ. The V antigen of Y. pestis is a secreted protein that is thought to act both as a regulatory protein and as a virulence factor. The V antigen has a key role in the Type III secretion process utilised by Y. pestis to translocate cytotoxic and anti-phagocytic Yersinia outer proteins (Yops) into the host cell. Supporting evidence for this role has been gained and the V antigen has been visualised on the bacterial cell surface (Jones et al., 2003).
      Both the rF1 and rV proteins, administered in alhydrogel, have been demonstrated to be highly immunogenic and protective against virulent plague in a number of animal models: mice, guinea pigs, and cynomolgus macaques (unpublished data). Further, the combination of rF1 plus rV is additive in the protection conferred on the vaccinee. In the mouse, the combined immunoglobulin G1 (IgG1) titer to rF1 plus rV has been shown to correlate with protection against challenge. Further, protection against plague in the mouse has been demonstrated by the passive transfer of antiserum specific for rF1 plus rV from immunized BALB/c mice into naïve SCID/beige mice (Williamson et al., 2005).
  • Preparation: The rF1 and rV antigens were produced in Escherichia coli from the expression systems previously described, under Good Manufacturing Practice conditions. The vaccine was formulated by adsorption to 20% (vol/vol) adjuvant at the required concentrations of each protein such that concentrations in the range 10 µg rF1 + 10 µg rV per ml up to 80 µg rF1 + 80 µg rV per ml were achieved in a final concentration of 0.26% (wt/vol) alhydrogel to achieve a molar ratio for rF1 to rV of 2:1. The formulated vaccine was designated rYP002 (Williamson et al., 2005).
  • Virulence:
  • Description: This vaccine utilizes a combination of the Fraction 1 antigen (F1) and the V antigen of Y. pestis in an optimum molar ratio. The F1 and V antigens, in recombinant form in this vaccine, are natural virulence factors of Y. pestis. Fraction 1 antigen, the major protein component of the capsule surrounding Y. pestis cells, is expressed only at 37 °C and it is believed to have anti-phagocytic activity. High anti-F1 titres have been correlated with survival following plague infection. Recombinant F1 antigen (rF1) has been produced by cloning the caf operon from Y. pestis into Escherichia coli and the protection provided by highly purified native F1 and recombinant F1 against Y. pestis has been demonstrated not to differ. The V antigen of Y. pestis is a secreted protein that is thought to act both as a regulatory protein and as a virulence factor. The V antigen has a key role in the Type III secretion process utilised by Y. pestis to translocate cytotoxic and anti-phagocytic Yersinia outer proteins (Yops) into the host cell. Supporting evidence for this role has been gained and the V antigen has been visualised on the bacterial cell surface (Jones et al., 2003).
    Both the rF1 and rV proteins, administered in alhydrogel, have been demonstrated to be highly immunogenic and protective against virulent plague in a number of animal models: mice, guinea pigs, and cynomolgus macaques (unpublished data). Further, the combination of rF1 plus rV is additive in the protection conferred on the vaccinee. In the mouse, the combined immunoglobulin G1 (IgG1) titer to rF1 plus rV has been shown to correlate with protection against challenge. Further, protection against plague in the mouse has been demonstrated by the passive transfer of antiserum specific for rF1 plus rV from immunized BALB/c mice into naïve SCID/beige mice (Williamson et al., 2005).
References
Jones et al., 2003: Jones SM, Griffin KF, Hodgson I, Williamson ED. Protective efficacy of a fully recombinant plague vaccine in the guinea pig. Vaccine. 2003 Sep 8; 21(25-26); 3912-8. [PubMed: 12922126].
Williamson et al., 2005: Williamson ED, Flick-Smith HC, Lebutt C, Rowland CA, Jones SM, Waters EL, Gwyther RJ, Miller J, Packer PJ, Irving M. Human immune response to a plague vaccine comprising recombinant F1 and V antigens. Infection and immunity. 2005 Jun; 73(6); 3598-608. [PubMed: 15908389].
S. typhi GroEL Protein Vaccine
Vaccine Information
  • Vaccine Name: S. typhi GroEL Protein Vaccine
  • Vaccine Ontology ID: VO_0004183
  • Type: Subunit vaccine
  • Status: Research
  • GroEL gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intramuscular injection (i.m.)
References
 
Salmonella IroN Protein Vaccine
Vaccine Information
  • Vaccine Name: Salmonella IroN Protein Vaccine
  • Vaccine Ontology ID: VO_0004184
  • Type: Subunit vaccine
  • Status: Research
  • IroN gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Intramuscular injection (i.m.)
References
 
Shiga Toxin 2 B Subunit Vaccine
Vaccine Information
  • Vaccine Name: Shiga Toxin 2 B Subunit Vaccine
  • Vaccine Ontology ID: VO_0004145
  • Type: Subunit vaccine
  • Antigen: The antigen for this vaccine is Shiga Toxin 2 B subunit (Marcato et al., 2001).
  • CS1 gene engineering:
    • Type: Recombinant protein preparation
    • Description: The Stx2 B subunit, which binds to globotriaosylceramide (GB3) receptors on target cells, was cloned. This involved replacing the Stx2 B subunit leader peptide nucleotide sequences with those from the Stx1 B subunit. The construct was expressed in the TOPP3 E. coli strain. The Stx2 B subunits from this strain assembled into a pentamer and bound to a GB3 receptor analogue. The cloned Stx2 B subunit was not cytotoxic to Vero cells or apoptogenic in Burkitt's lymphoma cells (Moravec et al., 2007).
    • Detailed Gene Information: Click Here.
  • StxB2 gene engineering:
    • Type: Recombinant protein preparation
    • Description: Shiga toxin 2 subunit B was used in the formation of a construct (Marcato et al., 2001).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Adjuvant:
    • VO ID: VO_0001267
    • Description: Quil‐A Saponin (Marcato et al., 2001).
  • Preparation: The vaccine contained cloned low endotoxin Stx2 B subunit preparation homogenized in an equal volume of adjuvant. The sham vaccine (used for a control) contained a 1:1 homogenate of Quil‐A and pyrogen‐free 0.9% NaCl irrigation solution (Marcato et al., 2001).
References
Marcato et al., 2001: Marcato P, Mulvey G, Read RJ, Vander Helm K, Nation PN, Armstrong GD. Immunoprophylactic potential of cloned Shiga toxin 2 B subunit. The Journal of infectious diseases. 2001; 183(3); 435-443. [PubMed: 11133375].
Moravec et al., 2007: Moravec T, Schmidt MA, Herman EM, Woodford-Thomas T. Production of Escherichia coli heat labile toxin (LT) B subunit in soybean seed and analysis of its immunogenicity as an oral vaccine. Vaccine. 2007 Feb 19; 25(9); 1647-57. [PubMed: 17188785].
soybean-expressed E. coli LTB vaccine
Vaccine Information
  • Vaccine Name: soybean-expressed E. coli LTB vaccine
  • Vaccine Ontology ID: VO_0000466
  • Type: Subunit vaccine
  • Antigen: Subunti B of E. coli heat labile enterotoxin LTB (Moravec et al., 2007).
  • eltB gene engineering:
    • Type: Expression of protein subunit
    • Description: The B subunit of the heat labile toxin of enterotoxigenic Escherichia coli (LTB) was used as a model immunogen for production in soybean seed. LTB expression was directed to the endoplasmic reticulum (ER) of seed storage parenchyma cells for sequestration in de novo synthesized inert protein accretions derived from the ER. Pentameric LTB accumulated to 2.4% of the total seed protein at maturity and was stable in desiccated seed(Moravec et al., 2007) .
    • Detailed Gene Information: Click Here.
  • FaeG gene engineering:
    • Type: Seed-specific protein expression
    • Description: A synthetic plant codon-optimized LTB gene and AAC60441, generously provided by A. Walmsley (Arizona Biodesign Institute) was modified by substitutions of the bacterial signal peptide with a 20 aa signal peptide from A. thaliana basic chitinase. A 14 aa extension comprising the FLAG epitope and KDEL ER retention signal, and flanking Bsp120 restriction sites were introduced by PCR. The final sequence encoded a 137 aa protein of 15.5 kDa that yielded a 13.3 kDa LTB-FLAG protein after signal peptide cleavage. Following subcloning into pGEM T/A (Promega) for sequence verification, the Bsp120 LTB gene fragment was subcloned into the pGly vector, placing it under the control of soybean seed-specific glycinin promoter and terminator [35]. The final soybean transformation vector pGly::ER-LTB contained a hygromycin selection marker (kindly provided by N. Murai, Lousiana State University) under the control of potato ubiquitin 3 promoter and terminator.
      LT is a hetero-oligomeric AB5 type enterotoxin composed of a 27 kDa A subunit with toxic ADP ribosyl transferase activity and a stable noncovalent-linked pentamer of 11.6 kDa B subunits. ETEC infection and colonization of the small intestine, and the production of LT, causes acute diarrhea that can be fatal without intervention. The ADP-ribosylation of Gsα, catalyzed by the A subunit, triggers increased intracellular cAMP levels that induce chloride efflux and fluid loss from intoxicated cells lining the small intestine. The B subunit pentamer mediates holotoxin binding to ganglioside GM1 on intestinal epithelial cells, with lower affinity for GD1B, asialoGM1 and lactosylceramide gangliosides (Moravec et al., 2007).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0000139
    • Description: In the event of s.c. immunization, LTB was administered in complete Freund's adjuvant (Moravec et al., 2007).
  • Preparation: For immunization, transgenic LTB-laden soybean seeds were ground in 5 vol. of PBS at 4 °C, the extracts were clarified by microcentrifugation at 20,000 × g for 5 min, and the total protein concentration was measured using the Bradford method (Moravec et al., 2007).
  • Virulence: Soy LTB was biochemically stable, functionally active and highly immunogenic (Moravec et al., 2007).
  • Description: Effective needle-free immunization strategies are needed to accommodate large-scale vaccination programs and avoid injection-related risks. To improve the efficacy of oral vaccination, antigens can be co-administered, or fused with a strong mucosal adjuvant. LT is a potent immunogen whose adjuvant active dose is well below its immunogenic dose. LT and detoxified mutants of LT trigger a stronger antibody response than LTB to co-administered antigens on a dose-for-dose basis. However, recombinant LTB is safely and commonly used as an adjuvant to stimulate antibody responses to co-administered protein antigens. LTB has also been used experimentally for the prevention and treatment of autoimmune diseases. Importantly, LTB has been shown to protect against the development of oral tolerance to co-fed soluble vaccine proteins, a serious consideration in the food-based delivery of vaccines. Transgenic plants offer the possibility to both produce and deliver an oral immunogen on a large-scale with low production costs and minimal purification or enrichment, and the potential exists for direct formulation of vaccines into animal feed and human consumables. Soybean has great potential as a vaccine delivery platform because of its naturally high protein content, nutritional value and multiple product streams (Moravec et al., 2007).
References
Moravec et al., 2007: Moravec T, Schmidt MA, Herman EM, Woodford-Thomas T. Production of Escherichia coli heat labile toxin (LT) B subunit in soybean seed and analysis of its immunogenicity as an oral vaccine. Vaccine. 2007 Feb 19; 25(9); 1647-57. [PubMed: 17188785].
Synthetic OMP1 Vaccine
Vaccine Information
  • Vaccine Name: Synthetic OMP1 Vaccine
  • Vaccine Ontology ID: VO_0004240
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: Lipidic amino acid-based synthetic peptides derived from the variable domains (VD) of Chlamydia trachomatis outer membrane protein 1 (Zhong et al., 1993).
  • Adjuvant:
  • Immunization Route: subcutaneous injection
References
Zhong et al., 1993: Zhong G, Toth I, Reid R, Brunham RC. Immunogenicity evaluation of a lipidic amino acid-based synthetic peptide vaccine for Chlamydia trachomatis. Journal of immunology (Baltimore, Md. : 1950). 1993; 151(7); 3728-3736. [PubMed: 7690812].
T. pallidum GlpQ Protein Vaccine
Vaccine Information
References
Cameron et al., 1998: Cameron CE, Castro C, Lukehart SA, Van Voorhis WC. Function and protective capacity of Treponema pallidum subsp. pallidum glycerophosphodiester phosphodiesterase. Infection and immunity. 1998; 66(12); 5763-5770. [PubMed: 9826352].
T. pallidum TmpB Protein Vaccine
Vaccine Information
  • Vaccine Name: T. pallidum TmpB Protein Vaccine
  • Vaccine Ontology ID: VO_0004025
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: Recombinant TmpB protein.
  • TmpB gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Subcutanteous and i.p.
References
 
T. pallidum Tp92 Protein Vaccine
Vaccine Information
References
Cameron et al., 2000: Cameron CE, Lukehart SA, Castro C, Molini B, Godornes C, Van Voorhis WC. Opsonic potential, protective capacity, and sequence conservation of the Treponema pallidum subspecies pallidum Tp92. The Journal of infectious diseases. 2000; 181(4); 1401-1413. [PubMed: 10762571].
Tripacel
Vaccine Information
  • Vaccine Name: Tripacel
  • Product Name: Pertussis Vaccine-Acellular, Combined with Diphtheria and Tetanus Toxoids (Adsorbed)
  • Tradename: Tripacel
  • Manufacturer: Sanofi Pasteur Ltd
  • Vaccine Ontology ID: VO_0010742
  • Type: Subunit vaccine
  • Status: Licensed
  • Location Licensed: Canada
  • Host Species for Licensed Use: Human
  • Adjuvant:
  • Preservative: 2-phenoxyethanol
  • Allergen: Latex in stopper
  • Immunization Route: Intramuscular injection (i.m.)
  • Storage: Store at at 2° to 8°C.
  • Approved Age for Licensed Use: 2 months up to 8 years of age.
References
 
Y. enterocolititica Subunit V Antigen Protein Vaccine
Vaccine Information
References
 
Y. pestis F1 antigen Vaccine with Flagellin
Vaccine Information
References
Honko et al., 2006: Honko AN, Sriranganathan N, Lees CJ, Mizel SB. Flagellin is an effective adjuvant for immunization against lethal respiratory challenge with Yersinia pestis. Infection and immunity. 2006; 74(2); 1113-1120. [PubMed: 16428759].
Y. pestis F1 protein vaccine
Vaccine Information
  • Vaccine Name: Y. pestis F1 protein vaccine
  • Vaccine Ontology ID: VO_0000829
  • Type: Subunit vaccine
  • Caf1 from Y. pestis biovar Microtus str. 91001 gene engineering:
    • Type: Protein
    • Detailed Gene Information: Click Here.
  • Adjuvant:
    • VO ID: VO_0001241
    • Description: Yersinia pestis fraction 1 capsular antigen (F1) is a plasmid (pFra)-encoded, proteinaceous capsule, synthesized in large quantities by the pathogen, and reported to confer antiphagocytic properties on Y. pestis by interfering with complementmediated opsonization. The protein is highly immunogenic and has been indirectly associated with eliciting a protective immune response in humans, as evidenced by the detection of high levels of anti-F1 antibody in F1-immunized volunteers (Andrews et al., 1996).
  • Preparation: Partially pure cell-associated (capsular) F1 was extracted and isolated. HIB containing xylose was inoculated with a loop of Y. pestis CO92 Pgm2 Lcr2 from a plate stock and grown. The bacteria were then harvested by centrifugation, and the supernatant was retained for isolation of cell-free F1. The cell pellets were next resuspended and recentrifuged before the supernatants were pooled. Crude cell-associated capsular F1 from the salt extract supernatants was precipitated with ammonium sulfate. Protein that precipitated was collected by centrifugation. Purified, detoxified Y. pestis and E. coli supernatant F1 and cell-extracted F1 were adsorbed to the adjuvant (Andrews et al., 1996).
  • Virulence:
  • Description: Yersinia pestis fraction 1 capsular antigen (F1) is a plasmid (pFra)-encoded, proteinaceous capsule, synthesized in large quantities by the pathogen, and reported to confer antiphagocytic properties on Y. pestis by interfering with complementmediated opsonization. The protein is highly immunogenic and has been indirectly associated with eliciting a protective immune response in humans, as evidenced by the detection of high levels of anti-F1 antibody in F1-immunized volunteers (Andrews et al., 1996).
References
Andrews et al., 1996: Andrews GP, Heath DG, Anderson GW Jr, Welkos SL, Friedlander AM. Fraction 1 capsular antigen (F1) purification from Yersinia pestis CO92 and from an Escherichia coli recombinant strain and efficacy against lethal plague challenge. Infection and immunity. 1996 Jun; 64(6); 2180-7. [PubMed: 8675324].
Y. pestis YscF Protein Vaccine
Vaccine Information
  • Vaccine Name: Y. pestis YscF Protein Vaccine
  • Vaccine Ontology ID: VO_0004157
  • Type: Subunit vaccine
  • Status: Research
  • YscF from Y. pestis CO92 gene engineering:
    • Type: Recombinant protein preparation
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: Subcutaneous Injection
References
 
Y. pestis YscF subunit vaccine
Vaccine Information
  • Vaccine Name: Y. pestis YscF subunit vaccine
  • Vaccine Ontology ID: VO_0000836
  • Type: Subunit vaccine
  • YscF from Y. pestis CO92 gene engineering:
    • Type: Protein
    • Description: YscF expressed and purified from E. coli was highly alpha-helical and formed relatively stable aggregates under physiological conditions.
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Preparation: To facilitate its purification, YscF was cloned into the overexpression plasmid pET24b (Novagen) to yield a hexahistidine-tag on the C-terminus of YscF (HT-YscF). Purified HT-YscF with the adjuvant was then used for innoculation (Matson et al., 2005).
  • Description: Due to the severity of plague and its potential for use as a bioweapon, better preventatives and therapeutics for plague are desirable. Subunit vaccines directed against the F1 capsular antigen and the V antigen (also known as LcrV) of Y. pestis are under development. However, these new vaccine formulations have some possible limitations: the F1 antigen is not required for full virulence of Y. pestis and LcrV has a demonstrated immunosuppressive effect. These limitations could damper the ability of F1/LcrV based vaccines to protect against F1-minus Y. pestis strains and could lead to a high rate of undesired side effects in vaccinated populations. Thus, the use of other antigens in a plague vaccine formulation may be advantageous. Desired features in vaccine candidates would be antigens that are conserved, essential for virulence and accessible to circulating antibody. Several of the proteins required for the construction or function of the type III secretion system (TTSS) complex could be ideal contenders to meet the desired features of a vaccine candidate. Accordingly, the TTSS needle complex protein, YscF, was selected to investigate its potential as a protective antigen (Matson et al., 2005).
References
Matson et al., 2005: Matson JS, Durick KA, Bradley DS, Nilles ML. Immunization of mice with YscF provides protection from Yersinia pestis infections. BMC microbiology. 2005 Jun 24; 5(1); 38. [PubMed: 15978133].
Yersinia PAV
Vaccine Information
  • Vaccine Name: Yersinia PAV
  • Vaccine Ontology ID: VO_0000833
  • Type: Subunit vaccine
  • Adjuvant:
  • Preparation: Fusion between the structural gene of staphylococcal protein A (PA) present on the vector plasmid pRIT5 and that of V antigen (LcrV) obtained from the lcr plasmid of Y. pseudotuberculosis resulted in the PA-V antigen peptide (PAV), encoded on pPAV13 carried by protease-deficient Escherichia coli BL21, which contained 305 N-terminal amino acids from PA plus 259 C-terminal amino acids from V antigen and could be purified to homogeneity in one step by immunoglobulin G affinity chromatography. Rabbit antibodies raised against one or more epitopes present within an internal portion of the V antigen domain of PAV have accounted for protection against experimental plague. PAV was diluted in phosphate buffer to 2 mg/ml and emulsified separately with an equal volume of the adjuvant (Nakajima et al., 1995).
  • Virulence:
References
Nakajima et al., 1995: Nakajima R, Motin VL, Brubaker RR. Suppression of cytokines in mice by protein A-V antigen fusion peptide and restoration of synthesis by active immunization. Infection and immunity. 1995 Aug; 63(8); 3021-9. [PubMed: 7622225].
YopE(67-77) Protein Vaccine
Vaccine Information
  • Vaccine Name: YopE(67-77) Protein Vaccine
  • Vaccine Ontology ID: VO_0004273
  • Type: Subunit vaccine
  • Status: Research
  • Antigen: YopE(69-77) peptide (Lin et al., 2011).
  • YopE gene engineering:
    • Type: Recombinant protein preparation
    • Description: YopE(69-77) protein was sythezised by New England Peptide (Gardner, MA) (Lin et al., 2011).
    • Detailed Gene Information: Click Here.
  • Adjuvant:
  • Immunization Route: intranasal immunization
References
Lin et al., 2011: Lin JS, Szaba FM, Kummer LW, Chromy BA, Smiley ST. Yersinia pestis YopE Contains a Dominant CD8 T Cell Epitope that Confers Protection in a Mouse Model of Pneumonic Plague. Journal of immunology (Baltimore, Md. : 1950). 2011; ; . [PubMed: 21653834].