Neisseria meningitidis 487 Meningococcus is spread through the exchange of saliva and other respiratory secretions during activities like coughing, kissing, and chewing on toys. Those with impaired immunity may be easier to get meningococcus. Meningococcal virulence is related to both capsule expression, expression of other surface structures, and underlying genotype. N meningitidis pathogenesis is related to its ability to express and modify capsule with serogroups A, B, C, W-135, X, and Y. Capsules of N meningitidis facilitate transmission and colonisation, and protect the meningococcus from desiccation, phagocytic killing, opsonisation, and complement-mediated bactericidal killing. Outer membrane proteins (e.g., PorB, PorA , Opa and Opc) contribute to meningococcal virulence. Outer membrane porins are involved in host-cell interactions and as targets for bactericidal antibodies. Endotoxin, or lipo-oligosaccharide, a major component of the outer membrane, differs in structure from enteric endotoxins and is crucial in inflammatory signalling via Toll-like receptor 4 (TLR4) (Stephens et al., 2007). Meningitis N. mengingitidis establishes systemic infections only in individuals who lack serum bacterial antibodies directed against the capsular or noncapsular (cell wall) antigens of the invading strain, or in patients deficient in the late-acting complement components. The presence of serum bactericidal IgG and IgM is probably the most important host factor in preventing invasive disease. The role of bactericidal antibodies in prevention of invasive disease explains why high attack rates are seen in infants from 6 to 9 months old, the time at which maternal antibodies are being lost. Individuals with complement deficiencies (C5, C6, C7, or C8) may develop meningococcemia despite protective antibody. This emphasizes the importance of the complement system in defense against meningococcal disease (Textbook of Bacteriology). It only infects humans; there is no animal reservoir. Neisseria meningitidis, also simply known as meningococcus, is a Gram-negative β-proteobacterium and member of the bacterial family Neisseriaceaeis. There are 13 serogroups based on different capsular polysaccharide structures. Among them, six serogroups (A, B, C, W-135, X, and Y) cause most life-threatening disease (Stephens et al., 2007). Baboon Papio cynocephalus 9556 Bank vole Clethrionomys glareolus 447135 Bear Ursus americanus 9643 Birds Passeroidea 175121 Brown Trout Salmo trutta 8032 Buffalo Bison bison 9901 Carnivores Vulpes 9625 Cat Felis catus 9685 Catfishes Siluriformes 7995 Cattle Bos taurus 9913 Chicken Gallus gallus 9031 Chimpanzee Pan troglodytes 9598 chinchillas Chinchillidae 10150 Copper Pheasant Syrmaticus soemmerringii 9067 Deer Cervus elaphus 9860 Deer mouse Peromyscus maniculatus 10042 Dog Canis familiaris 9615 Ducks Anas 8835 Ferret Mustela putorius furo 9669 Fish Hyperotreti 117565 Gerbil Gerbillina 10045 Goat Capra hircus 9925 Gray wolf Canis lupus 9612 Guinea pig Cavia porcellus 10141 Hamster Mesocricetus auratus 10036 Horse Equus caballus 9796 Human Homo sapiens 9606 Macaque Macaca fascicularis 9541 Mongolian Gerbil Meriones unguiculatus 10047 Monkey Platyrrhini 9479 Mouse Mus musculus 10090 None None Parrot Psittacidae 9224 Pig Sus scrofa 9823 Rabbit Oryctolagus cuniculus 9986 Rainbow trout Oncorhynchus mykiss 8022 Rat Rattus 10114 Raven Corvus corax 56781 sei whale Balaenoptera borealis 9768 Sheep Ovis aries 9940 Squirrel Spermophilus richardsonii 37591 Tree shrew Tupaiidae 9393 Trouts, salmons & chars Salmoninae 504568 Turkey Meleagris gallopavo 9103 Vole Microtus ochrogaster 79684 Water buffalo Bubalus bubalis 391902 5CVMB VO_0011348 Subunit vaccine Licensed Intraperitoneal injection (i.p.) aluminum hydroxide combined with CpG oligonucleotides (Giuliani et al., 2006) Intraperitoneal injection (i.p.) Five antigens are included: GNA2132, GNA1870, NadA, GNA1030, and GNA2091 (Giuliani et al., 2006) BEXSERO Meningococcal Group B Vaccine BEXSERO Novartis Vaccines and Diagnostics, Inc VO_0003066 Subunit vaccine Licensed Intramuscular injection (i.m.) USA, Canada BEXSERO (Meningococcal Group B Vaccine) is a sterile, white, opalescent, suspension for intramuscular injection. Each 0.5 mL dose of BEXSERO is formulated to contain 50 micrograms each of recombinant proteins Neisserial adhesin A (NadA), Neisserial Heparin Binding Antigen (NHBA), and factor H binding protein (fHbp), 25 micrograms of Outer Membrane Vesicles (OMV), 1.5 mg aluminum hydroxide (0.519 mg of Al3+), 3.125 mg sodium chloride, 0.776 mg histidine, and 10 mg sucrose at pH 6.4 – 6.7.(FDA: BEXSERO) Aluminum hydroxide Store at 2°C to 8°C (36°F to 46°F), do not freeze, and keep away from light. Intramuscular injection (i.m.) CCPS-P64kR VO_0004165 Conjugate vaccine Research Not specified Al(OH)3 (Carmenate et al., 2004). Not specified Recombinant protein preparation Rat pups, aged 5 or 6 days, were injected i.p. with 100 μl of sera ( from immunized mice) previously diluted 1:10 and ferric dextran (Carmenate et al., 2004). Sera of the challenge group of mice immunized with CCPS-P64kR showed a three-fold higher bactericidal response than the sera of the group immunized with the plain CCPS and they were able to protect against challenge with Neisseria meningococci in the infant rat protection model (Carmenate et al., 2004). One hour after immunization, infant rats were challenged with 10^7 cfu of meningococcal strain Z4181. The development of bacteremia was assessed by culturing the blood samples taken 4 h after challenge (Carmenate et al., 2004). BALB/c Two experiments were carried out; in both cases mice were immunized with 2.5 μg of either plain or conjugated CCPS, and Al(OH)3 as adjuvant. Two doses were given 15 days apart and 7 days after the last dose mice were bled, sera were stored at −20°C. In the first experiment four groups of 10 mice each were immunized with the following immunogens: CCPS–P64kR, CCPS–P64kC, carrier protein P64k, and plain polysaccharide. For the second experiment, four groups of 10 mice each were immunized with the three conjugates obtained from different size polysaccharides using the reductive amination method and with plain CCPS as control (Carmenate et al., 2004). Sera of the challenge group immunized with CCPS-P64kR showed a three-fold higher bactericidal response than the sera of the group immunized with the plain CCPS and they were able to protect against challenge with Neisseria meningococci in the infant rat protection model (Carmenate et al., 2004). Sera of immunized mice was used in rats to detect an immune response (Carmenate et al., 2004). licensed Meningococcal disease human vaccine Generic Unknown VO_0000053 Conjugate vaccine Licensed A generic representation of vaccines used to prevent meningococcal disease in humans, most commonly formulated as conjugate vaccines that link polysaccharide antigens from Neisseria meningitidis to carrier proteins to enhance immunogenicity. These vaccines are widely licensed and have significantly reduced the incidence of meningitis caused by meningococcal bacteria. Menactra Meningococcal Polysaccharide (Serogroups A, C, Y and W-135) Diphtheria Toxoid Conjugate Vaccine Menactra Sanofi Pasteur Inc. VO_0000071 Conjugate vaccine Licensed Intramuscular injection (i.m.) USA (License #1725), Canada Contains Neisseria meningitidis serogroup A, C, Y and W-135 capsular polysaccharide antigens individually conjugated to diphtheria toxoid protein. Menactra vaccine is not indicated for immunization against diphtheria (FDA: Menactra). Store at 2° to 8°C (35° to 46°F). DO NOT FREEZE. Cultured on Mueller Hinton agar and grown in Watson Scherp media. The polysaccharides are extracted from the N meningitidis cells and purified by centrifugation, detergent precipitation, alcohol precipitation, solvent extraction and diafiltration (FDA: Menactra). Intramuscular injection (i.m.) Clinical studies reported antibodies were seen in 90-100% of those who were vaccinated with Menactra (FDA: Menactra). Side effects of vaccination include: injection site reactions, headache, fatigue, irritability and fever. MenHibrix Meningococcal Groups C and Y and Haemophilus b Tetanus Toxoid Conjugate Vaccine MenHibrix GlaxoSmithKline Biologicals VO_0000031 Conjugate vaccine Licensed Intramuscular injection (i.m.) United States Intramuscular injection (i.m.) Neisseria meningitidis serogroup C and Y capsular polysaccharide antigens and Haemophilus b capsular polysaccharide (polyribosyl-ribitol-phosphate [PRP]) (FDA: MenHibrix). Meningitec Meningococcal Group C Conjugate Vaccine (Diphtheria CRM197 Protein) Meningitec Berna Biotech, Wyeth Canada VO_0010724 Subunit vaccine Licensed Intramuscular injection (i.m.) Canada Products: Conjugate. Aluminum phosphate 2°C to 8°C (36°F to 46°F). Intramuscular injection (i.m.) Meningococcal Polysaccharide Vaccine, Groups A & C, Menomune A/C Meningococcal Polysaccharide Vaccine, Groups A & C, Menomune A/C Sanofi Pasteur Ltd VO_0010725 Subunit vaccine Licensed Subcutaneous injection Canada Products: Polysaccharide. Other components: Lactose. Store at at 2° to 8°C (35° to 46°F). Subcutaneous injection Menjugate Meningococcal Group C CRM-197 Conjugate Vaccine Menjugate Novartis Vaccines and Diagnostics VO_0010726 Conjugate vaccine Licensed Intramuscular injection (i.m.) Canada Products: Conjugate. Aluminum hydroxide Do not store above 25° C. Intramuscular injection (i.m.) Menomune-A/C/Y/W-135 Meningococcal Polysaccharide Vaccine, Groups A, C, Y, W135 Combined Menomune-A/C/Y/W-135 Sanofi Pasteur, Inc. VO_0000072 Live, attenuated vaccine Licensed subcutaneous injection USA (License #1725) Meningococcal Polysaccharide Vaccine, Groups A, C, Y and W-135 Combined, is indicated for active immunization against invasive meningococcal disease caused by these serogroups (FDA: Menomune– A/C/Y/W-135). Store the freeze-dried vaccine and reconstituted vaccine, when not in use, at 2° to 8°C (35° to 46°F). MEMOMUNE is cultivated with Mueller Hinton agar and Watson Scherp media and is freeze-dried with the group-specific polysaccharide antigens from Neisseria meningitidis, Group A, Group C, Group Y and Group W-135 (FDA: Menomune– A/C/Y/W-135). subcutaneous injection Meningococcal Polysaccharide Vaccine, Groups A, C, Y and W-135 Combined Measurable levels of antibodies against the group A and C polysaccharides decrease markedly during the first 3 years following a single dose of vaccine (FDA: Menomune– A/C/Y/W-135). The serogroup A polysaccharide induces and antibody response in children as young as 3 months of age, the serogroup C component can be poorly immunogenic in recipients who are less than 18 to 24 months of age 5. The serogroups A and C have demonstrated estimated clinical efficacies of 85% to 100% in older children and adults. Serogroups Y and W-135 polysaccharides are safe and immunogenic in adults and in children greater than 2 years of age (FDA: Menomune– A/C/Y/W-135). Side effects of vaccination include: pain and redness of injection site, fever and/or headache (FDA: Menomune– A/C/Y/W-135). Menveo Meningococcal (Groups A, C, Y and W-135) Oligosaccharide Diphtheria CRM197 Conjugate Vaccine Menveo Novartis Vaccines and Diagnostics, Inc. VO_0001246 Conjugate vaccine Licensed Intramuscular injection (i.m.) USA, Canada MENVEO [Meningococcal (Groups A, C, Y and W-135) Oligosaccharide Diphtheria CRM197 Conjugate Vaccine] is a sterile liquid vaccine administered by intramuscular injection that contains N. meningitidis serogroup A, C, Y and W-135 oligosaccharides conjugated individually to Corynebacterium diphtheriae CRM197 protein (FDA: Menveo). Store refrigerated, away from the freezer compartment, at 36°F to 46°F (2°C to 8°C). Keep away from light (FDA: Menveo). The polysaccharides are produced by bacterial fermentation of N. meningitidis (serogroups A, C, Y or W-135). N. meningitidis strains A, C, Y and W-135 are each cultured and grown on Franz Complete medium and treated with formaldehyde. MenA, MenW-135 and MenY polysaccharides are purified by several extraction and precipitation steps. MenC polysaccharide is purified by a combination of chromatography and precipitation steps. The protein carrier (CRM197) is produced by bacterial fermentation and is purified by a series of chromatography and ultrafiltration steps. C. diphtheriae is cultured and grown on CY medium containing yeast extracts and amino acids. The oligosaccharides are prepared for conjugation from purified polysaccharides by hydrolysis, sizing, and reductive amination. After activation, each oligosaccharide is covalently linked to the CRM197 protein. The resulting glycoconjugates are purified to yield the four drug substances, which compose the final vaccine (FDA: Menveo). Intramuscular injection (i.m.) N. meningitidis serogroup A, C, Y and W-135 oligosaccharides conjugated individually to Corynebacterium diphtheriae CRM197 protein (FDA: Menveo). N. meningitidis DNA vaccine P3A VO_0004569 DNA vaccine Research pcDNA3.1 [Ref2700:Prinz et al., 2003] Intramuscular injection (i.m.) aluminium-phosphate gel adjuvant (Prinz et al., 2003) Intramuscular injection (i.m.) a T-cell helper epitope and a peptide mimic of N. meningitidis serogroup C (Prinz et al., 2003) DNA vaccine construction The T-cell epitope used was from HIV gp120 (Prinz et al., 2003). Mice immunized with P3A DNA produced an anti-MCPS IgM antibody response that was significantly higher (P < 0.05) than that of mice immunized with P3C DNA (negative control) (Prinz et al., 2003). VO_0003057 Mice immunized with P3A DNA were protected against meningococcal infection, with 100% survival. Five of the six mice immunized with P3C DNA (negative control) died within 24 hr postchallenge (Prinz et al., 2003). N. meningitidis ExbB Protein Vaccine VO_0004011 Subunit vaccine Research Subcutaneous injection Freund's incomplete adjuvant (Sun et al., 2005). Subcutaneous injection Recombinant protein preparation BALB/c To examine the protective efficacy of recombinant proteins, adult mice (6-week-old, female BALB/c animals, 35 per group) were immunised on days 1 and 21 with 25 μg of antigen given by subcutaneous (s.c.) injection. Each protein was mixed with Freund's incomplete adjuvant (50% v/v) prior to administration. Mice in control groups were immunised with adjuvant alone or recombinant homologous PorA prior to challenge (Sun et al., 2005). ExbB, which is required for iron acquisition, elicited protective immunity and was able to protect mice from bacterial challenge (Sun et al., 2005). 28 days after immunization, animals were challenged with live bacteria at either a high (10^7 CFU, 15 mice) or low (10^6 CFU, 15 mice) dose of MC58 (Sun et al., 2005). N. meningitidis LctP Protein Vaccine VO_0004012 Subunit vaccine Research Subcutaneous injection Freund's incomplete adjuvant (Sun et al., 2005). Subcutaneous injection Recombinant protein preparation BALB/c To examine the protective efficacy of recombinant proteins, adult mice (6-week-old, female BALB/c animals, 35 per group) were immunised on days 1 and 21 with 25 μg of LctP given by subcutaneous (s.c.) injection. Each protein was mixed with Freund's incomplete adjuvant (50% v/v) prior to administration. Mice in control groups were immunised with adjuvant alone or recombinant homologous PorA prior to challenge (Sun et al., 2005). LctP which is required for iron acquisition, elicited protective immunity and was able to protect mice from bacterial challenge (Sun et al., 2005). 28 days after immunization, animals were challenged with live bacteria at either a high (10^7 CFU, 15 mice) or low (10^6 CFU, 15 mice) dose of MC58 (Sun et al., 2005). N. meningitidis NspA Protein Vaccine VO_0004013 Subunit vaccine Research Intraperitoneal injection (i.p.) QuilA (CedarLane Laboratories, Hornby, Ontario, Canada) (Martin et al., 1997). Intraperitoneal injection (i.p.) Recombinant protein preparation Groups of mice were injected three times at 3-wk intervals with 10 or 20 μg of affinity-purified NspA recombinant protein and 25 μg of QuilA (CedarLane Laboratories, Hornby, Ontario, Canada) as the adjuvant. Control mice were injected with either 20 μg of BSA (Sigma), concentrated E. coli BL21(DE3) supernatant, or PBS. 2 wk after the third injection the mice were used for the protection experiments (Martin et al., 1997). 80% of the mice immunized with three injections of either 10 or 20 μg of purified recombinant meningococcal NspA protein survived the bacterial challenge comparatively to 0 to 20% in the control groups. Survivors at 72 h did not succumb during an additional two weeks of observation. The mice in the control group injected with concentrated E. coli culture supernatant were not protected against the bacterial challenge indicating that the components present in the culture media and other E. coli antigens that might be present in small amounts after purification do not contribute to the observed protection against N. meningitidis (Martin et al., 1997). For inoculation of mice, meningococci were removed from the chocolate agar plates after ∼20 h of incubation and suspended in PBS and injected into mice (Martin et al., 1997). N. meningitidis TbpA Protein Vaccine VO_0004064 Subunit vaccine Research subcutaneous injection 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). subcutaneous injection rTbpA Recombinant protein preparation NIH Each mouse received 0.2 ml, containing 10 μg of rTbpA protein and Freund's complete adjuvant, by subcutaneous injection. All animals were immunized on days 1, 21, and 28 (West et al., 2001). 100% protection was afforded by vaccination with rTbpA at the 2 × 10^7 CFU challenge dose andat the 2 × 10^8 CFU challenge dose, the rTbpA-vaccinated group had an 85% survival rate (West et al., 2001). Mice were infected by intraperitoneal injection of N. meningitidis at several challenge doses (West et al., 2001). N. miningitidis TBP2 Protein Vaccine VO_0004014 Subunit vaccine Research Subcutaneous Injection Aluminum hydroxide (Lissolo et al., 1995). Subcutaneous Injection Recombinant protein preparation Groups of 48 mice were immunized subcutaneously on days 0, 21, and 35 with different vaccine preparations containing 5 mg of protein adsorbed onto 0.1 mg of aluminum hydroxide per 0.5 ml; PBS containing aluminum hydroxide and heat-inactivated N. meningitidis B16B6 were used as controls (Lissolo et al., 1995). Mice immunized with purified Tbp2 survived a lethal challenge to a similar degree as animals immunized with the Tbp1-Tbp2 complex, demonstrating that Tbp2 played an important role in the protective activity observed with the complex, eliciting antibodies that are not only bactericidal but also inhibitory for meningococcal growth (Lissolo et al., 1995). 41 days after immunization, mice within a group were subdivided into groups of eight, and each subgroup received by the intraperitoneal route 24 mg of iron-loaded hTf (Sigma) and, immediately after by the intraperitoneal route, 0.5 ml of N. meningitidis grown under iron restriction. The bacterial load varied from 10^4 to 10^8 CFU. Mortality rates were measured for 5 days following challenge (Lissolo et al., 1995). Neisseria meningitidis metH/siaD mutant vaccine VO_0002858 Live, attenuated vaccine Research Intraperitoneal injection (i.p.) Intraperitoneal injection (i.p.) Gene mutation This metH/siaD mutant is from Neisseria meningitidis (Li et al., 2004). Gene mutation This metH/siaD mutant is from Neisseria meningitidis (Li et al., 2004). Gene mutation This metH/siaD mutant is from Neisseria meningitidis (Li et al., 2004). A metH/siaD mutant is attenuated in mice (Li et al., 2004). A metH/siaD mutant induces significant protection in mice from challenge with wild type neisseria meningitidis (Li et al., 2004). Neisseria meningitidis rfaF/siaD mutant vaccine VO_0002859 Live, attenuated vaccine Research Intraperitoneal injection (i.p.) Intraperitoneal injection (i.p.) Gene mutation This rfaF/siaD mutant is from Neisseria meningitidis (Li et al., 2004). Gene mutation This rfaF/siaD mutant is from Neisseria meningitidis (Li et al., 2004). A rfaF/siaD mutant is attenuated in mice (Li et al., 2004). An rfaF/siaD mutant induces significant protection in mice from challenge with wild type Neisseria meningitidis (Li et al., 2004). Neisvac-C Meningococcal Group C-TT Conjugate Vaccine, Adsorbed Neisvac-C Baxter Healthcare Corporation, GlaxoSmithKline VO_0010729 Conjugate vaccine Licensed Intramuscular injection (i.m.) Canada Products: Conjugate. Aluminum hydroxide Store at 2°C to 8°C. Intramuscular injection (i.m.) NIMENRIX Meningococcal polysaccharide groups A, C, W-135 and Y conjugate vaccine NIMENRIX Pfizer Inc. VO_0003080 Conjugate vaccine Licensed Intramuscular injection (i.m.) Canada NIMENRIX® (meningococcal polysaccharide groups A, C, W-135 and Y conjugate vaccine) is a tetravalent meningococcal polysaccharide conjugated vaccine consisting of Neisseria meningitidis capsular polysaccharides A, C, W-135 and Y each coupled to tetanus toxoid as a carrier protein. The Neisseria meningitidis serogroups A and C polysaccharides are conjugated with an adipic dihydrazide (AH) spacer and indirectly conjugated to the tetanus toxoid whereas the W-135 and Y polysaccharides are conjugated directly to tetanus toxoid. (Pfizer: NIMENRIX) Store at 2°C to 8°C (36°F to 46°F), do not freeze, and protect from light. Intramuscular injection (i.m.) TRUMENBA Meningococcal Group B Vaccine TRUMENBA Pfizer Inc. VO_0003081 Subunit vaccine Licensed Intramuscular injection (i.m.) USA Trumenba is a sterile suspension composed of two recombinant lipidated factor H binding protein (fHBP) variants from N. meningitidis serogroup B, one from fHBP subfamily A and one from subfamily B (A05 and B01, respectively). The proteins are individually produced in E. coli. Production strains are grown in defined fermentation growth media to a specific density. The recombinant proteins are extracted from the production strains and purified through a series of column chromatography steps. Polysorbate 80 (PS80) is added to the drug substances and is present in the final drug product. (FDA: TRUMENBA) Aluminum phosphate Store at 2°C to 8°C (36°F to 46°F), do not freeze. Intramuscular injection (i.m.) ExbB Neisseria meningitidis MC58 VO_0011186 903370 15677575 NMB1729 AE002098 NP_274732 122586 1812128 1812790 - biopolymer transport protein 9.81 22358.4 220 identified by similarity to EGAD:145333; match to protein family HMM PF01618 >NC_003112.2:1812128-1812790 Neisseria meningitidis MC58 chromosome, complete genome ATCAGCTATCCTTTTGATTAAGCAGGCGGACGTGCAAATCGTGCGCCATCGCATCCAAATCCTGGGTCAG TATTTTTGTGCCGCGATTGAGGAAGTTGTATGCCAACACCGCCGGAATCGCCACGAACAAACCCGCCGCC GTCGCCACCAGTGCCTCGCCAATCGGGCCGGCAACCGCCGCAATACTCATCTGCCCGCTTTGCCCGATAT TGATCAGGGCGTGGTAAATCCCCCAAACCGTGCCGAACAGCCCGATAAACGGCGCGGTCGCGCCGATGGA GGCAAGCGCGGTCATCCCGTAATCAAACCGGCGCATAATCTGCGCCATACTGTTGCGGATTTGAATGACC AAATACTCGTTCAACGGCAAAGCCTGCGCCAGTTCGGACGCTTCGTTTCGGCGGTAGTTGCGGTAAGACT GCAATGCCTCTTGCGCCAGTTTGGACAAAGGCGCATCGACGGCGCGCACTTTTTCGACCGCGTCGTTCAG CGACAAAGTATCGCGCATATGCCGTTTGACGGCGGCATTCCCTTTGCGCGCCCGATACAGCTTGATGCAG CGCAAGACAACCAAACACCACGTTACGATACTCATCAACAGCATCAACACAAACACACCAATCAGGACGG GATCGCCCGATTCAAACACTAATTTCAAATTCA >NP_274732.1 biopolymer transport protein [Neisseria meningitidis MC58] MNLKLVFESGDPVLIGVFVLMLLMSIVTWCLVVLRCIKLYRARKGNAAVKRHMRDTLSLNDAVEKVRAVD APLSKLAQEALQSYRNYRRNEASELAQALPLNEYLVIQIRNSMAQIMRRFDYGMTALASIGATAPFIGLF GTVWGIYHALINIGQSGQMSIAAVAGPIGEALVATAAGLFVAIPAVLAYNFLNRGTKILTQDLDAMAHDL HVRLLNQKDS Protective antigen A total of 11 meningococcal proteins that are necessary for establishing systemic infection were expressed as recombinant antigens and assessed for their ability to protect mice against live bacterial challenge against N. meningitidis; ExbB, which is required for iron acquisition, elicited protective immunity [Ref1198:Sun et al., 2005]. gp120 Human immunodeficiency virus 1 2326505 CDD:278917 GOA:O40515 InterPro:IPR000777 UniProtKB/TrEMBL:O40515 11676 ? 9.81 11668 172 Envelope glycoprotein GP120; pfam00516 >CAA74764.1 gp120, partial [Human immunodeficiency virus 1] NGSLAEGEVVIRSENFTDNAKTIIVQLNESVVINCTRPNNNTRKNIHLGRGRSVYATEKIIGNVKQAHCN ISRAKWNDTLKQIVEKLREQFGKNKTIVFNQSSGGDPEI Protective antigen he DNA construct induced a significant anti-polysaccharide antibody response that was bactericidal. Mice immunized with the DNA construct were subsequently protected against challenge with a lethal dose of N. meningitidis serogroup C.[Ref2700:Prinz et al., 2003] lctP Neisseria meningitidis VO_0011185 254667969 CDD:224535 EnsemblGenomes-Gn:NMO_0425 EnsemblGenomes-Tr:CBA04244 GOA:C6S5G4 InterPro:IPR003804 UniProtKB/TrEMBL:C6S5G4 662598 ? L-lactate permease 8.92 52305.14 601 L-lactate permease [Energy production and conversion]; COG1620 >CBA04244.1 L-lactate permease [Neisseria meningitidis alpha14] MALFLSIFPIVLLIWLMVKKNSMPSYVALPITAVLIYAIKLFYFGDAGMLLNATAASGLVKTLTPITVIF GAIMFNRMMETTGCIDVIRKWLATISPNPVAQLMIIGWAFAFMIEGASGFGTPAAIAAPILMSLGFNPLK VAIFTLVMNSVPVSFGAVGTPTWFGFAPLNLSAEDILAIGRQTGVMHFFAGFVIPVIGLGFIVPWSEIRK NLGFVAIAVFSCTIPYVALAMVNEEFPSLVAGAIGLMVSVFAANQGWGLSKDHAKDPNAEKVPFAQVAKA LAPLGMLIGMLVVTRIKQLGIKGILTSKEEWFSFQLPFDLSKITVSDSLTITFGNIFGQDVSASYQTLYV PAWIPFVLTVWICILLYKTKFKDAWTIYSVTFNQTKKPLLALMGALIMVQLMLVGGDNSMVKIIGKEFAA MAGEHWVYFSPYLGAIGAFFSGSNTVSNLTFGPIQQQIALDTGLSVTLILALQSVGGAMGNMVCLNNIIA VCTVLDVKNSEGAIIKKTVIPMAIYGVIAVVAAMIFFL Protective antigen A total of 11 meningococcal proteins that are necessary for establishing systemic infection were expressed as recombinant antigens and assessed for their ability to protect mice against live bacterial challenge against N. meningitidis; the lactate permease (LctP) elicited protective immunity [Ref1198:Sun et al., 2005]. lpdA Neisseria meningitidis VO_0011181 1017430 CDD:133458 CDD:304358 CDD:180579 CDD:278498 CDD:280934 GOA:Q51191 HSSP:1OJT InterPro:IPR000089 InterPro:IPR000815 InterPro:IPR001327 InterPro:IPR003016 InterPro:IPR004099 InterPro:IPR006258 InterPro:IPR011053 InterPro:IPR012999 InterPro:IPR013027 InterPro:IPR016156 UniProtKB/TrEMBL:Q51191 487 ? outer membrane protein P64k or PM-6 4.94 56755.94 685 Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid...; cd06849 >CAA57206.1 outer membrane protein P64k or PM-6, partial [Neisseria meningitidis] MALVELKVPDIGGHENVDIIAVEVNVGDTIAVDDTLITLETDKATMDIPAEVAGVVKEVKVKVGDKISEG GLIVVVEAEGAATAPKAEAPATPAQEAPKAAAPAPQAAQFGGSADAEYDVVLGGGPGGYSAAFAAADEGL KVAIVERYKTLGGVCLNVGCIPSKALLHNAAVIDEVRHLAANGIKYPEPELDIDMLRAYKNGVVSRLTGG LAGMAKRRKVDVIQGDGQFLDPHHLEVSLTAGDAYEQAAPTGEKKIVAFKNCIIAAGSRVTKLPFIPEDP RIIDSSGALALKEVPGKLLIIGAGIIGLEMGTVYSTLGSRLDVVEMMDGLMQGADRDLVKVWQKQNEYRF DNIMVNTKTVAVEPKEDGVYVTFEGANAPKEPQRYDAVLVAAGRAPNGKLISAEKAGVAVTDRGFIEVDK QMRTNVPHIYAIVDIVGQPMLAHKAVHEGHVAAENCAGHKAYFDARVIPGVAYTSPEVAWVGETELSAKA SGRKITKANFPWAASGRAIANGCDNGFTKLIFDAETGRIIGGGIVGPNGGDMIGEVCLAIEMGCDAADIG KTIHPHPTLGESIGMAAEVALGTCTDLPPQKKK Other Sera of the challenge group immunized with CCPS-P64kR showed a three-fold higher bactericidal response than the sera of the group immunized with the plain CCPS and they were able to protect against challenge with Neisseria meningococci in the infant rat protection model [Ref1194:Carmenate et al., 2004]. metH Neisseria meningitidis MC58 903064 15676837 NMB0944 AE002098 NP_273982 122586 957284 959560 + 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase 5.08 79718.7 758 catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine to form methionine >gi|77358697:957284-959560 Neisseria meningitidis MC58, complete genome CATGACAACATTACATTTCTCAGGCTTCCCGCGTGTCGGCGCCTTCCGCGAATTGAAATTCGCACAAGAA AAATACTGGCGCAAAGAAATCAGCGAGCAAGAATTGCTGGCTGTTGCTAAAGACTTGCGCGAGAAAAACT GGAAACACCAGGTCGCTGCCAACGCCGATTTCGTTGCCGTAGGCGATTTCACTTTCTACGACCACATCCT CGACCTGCAAGTCGCCACCGGCGCGATTCCCGCCCGCTTCGGCTTCGACAGCCAAAACCTGTCTTTGGAA CAATTCTTCCAACTGGCGCGCGGTAACAAAGACCAATTCGCTATCGAAATGACCAAATGGTTCGACACCA ACTACCACTACTTGGTGCCTGAATTCCACGCCGATACCGAATTCAAAGCCAATGCCAAACACTATGTTCA ACAACTGCAAGAAGCCCAAGCCCTCGGTCTGAAAGCCAAACCGACCGTTGTAGGTCCGTTGACTTTCCTG TGGGTGGGTAAAGAAAAAGGCGCCGTCGAATTCGACCGTCTGAGCCTGTTGCCTAAACTGTTGCCTGTTT ACGTTGAAATCCTGACTGCTTTGGTTGAAGCCGGTGCCGAGTGGATTCAAATCGACGAGCCTGCTTTGGC TGTCGATTTGCCTAAAGAATGGGTGGAAGCCTACAAAGACGTTTACGCTACTTTGAGCAAAGTAAGTGCC AAAATCCTGTTGAGCACTTACTTCGGTTCTGTTGCCGAACACGCCGCATTGTTGAAAGCCCTGCCTGTTG ACGGTCTGCACATCGACTTGGTACGCGCCCCCGAGCAACTGGACGCGTTCGCCGACTACGACAAAGTCCT GTCTGCCGGCGTGATTGACGGCCGCAACATTTGGCGCGCCAACCTGAACAAAGTTTTGGAAACTGTCGAG CCTCTGCAAGCCAAACTGGGTGACCGTTTGTGGATTTCCAGCTCTTGCTCGCTGCTGCACACTCCATTTG ACTTGTCAGTTGAAGAAAAACTGAAAGCCAACAAACCCGACCTGTACTCTTGGTTGGCATTCACCCTGCA AAAAACCCAAGAATTGCGCGTTCTGAAAGCTGCATTGAACGAAGGCCGTGATTCTGTTGCCGAAGAACTC GCCGCCAGCCAAGCTGCTGCCGACTCCCGTGCCAACAGCAGCGAAATCCATCGTGCAGACGTTGCCAAAC GCCTGGCCGATTTGCCTGCCAACGCAGACCAACGCAAATCTCCATTTGCCGACCGTATCAAAGCGCAACA AGCATGGTTGAACCTACCTCTGCTACCGACTACCAACATCGGTTCTTTCCCGCAAACCACCGAAATCCGC CAGGCACGCTCAGCCTTCAAAAAAGGCGAACTGTCTGCCGCCGATTACGAAGCCGCGATGAAAAAAGAAA TCGCCTTGGTGGTTGAAGAGCAAGAAAAACTGGACTTGGACGTACTGGTACACGGCGAAGCCGAGCGTAA CGACATGGTTGAATACTTCGGCGAATTGTTGAGCGGTTTTGCATTCACTCAATACGGCTGGGTACAAAGC TACGGCTCACGCTGCGTGAAACCACCGATTATCTTTGGCGACGTAAGCCGTCCTGAAGCCATGACCGTGG CTTGGTCTACTTACGCACAAAGCCTGACCAAACGCCCGATGAAAGGTATGTTGACCGGCCCTGTAACCAT TCTGCAATGGTCTTTCGTCCGCAACGACATTCCTCGCTCTACCGTGTGCAAACAAATCGCACTGGCTCTG AACGACGAAGTATTGGATCTGGAAAAAGCCGGCATCAAAGTCATCCAAATTGACGAACCTGCCATCCGCG AAGGCTTGCCGCTGAAACGCGCCGATTGGGATGCCTACCTGAACTGGGCGGGCGAATCCTTCCGCCTGTC CTCTGCCGGTTGCGAAGACAGCACCCAAATCCACACTCATATGTGTTACTCCGAGTTCAACGATATCCTG CCTGCGATTGCTGCAATGGATGCGGACGTGATCACCATCGAGACTTCACGTTCCGACATGGAACTCTTGA CCGCGTTCGGCGAATTCCAATACCCGAACGACATCGGCCCGGGGGTTTACGACATCCACAGCCCGCGCGT ACCGACAGAAGCCGAAGTGGAGCACCTGTTGCGCAAAGCCATCGAGGTTGTACCGGTTGAACGTCTGTGG GTTAACCCGGACTGCGGCCTGAAAACACGCGGCTGGAAAGAAACTCTGGAACAACTCCAAGTAATGATGA ACGTAACCCGAAAACTGCGTGCCGAATTGGCGAAATA >gi|15676837|ref|NP_273982.1| 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase [Neisseria meningitidis MC58] MTTLHFSGFPRVGAFRELKFAQEKYWRKEISEQELLAVAKDLREKNWKHQVAANADFVAVGDFTFYDHIL DLQVATGAIPARFGFDSQNLSLEQFFQLARGNKDQFAIEMTKWFDTNYHYLVPEFHADTEFKANAKHYVQ QLQEAQALGLKAKPTVVGPLTFLWVGKEKGAVEFDRLSLLPKLLPVYVEILTALVEAGAEWIQIDEPALA VDLPKEWVEAYKDVYATLSKVSAKILLSTYFGSVAEHAALLKALPVDGLHIDLVRAPEQLDAFADYDKVL SAGVIDGRNIWRANLNKVLETVEPLQAKLGDRLWISSSCSLLHTPFDLSVEEKLKANKPDLYSWLAFTLQ KTQELRVLKAALNEGRDSVAEELAASQAAADSRANSSEIHRADVAKRLADLPANADQRKSPFADRIKAQQ AWLNLPLLPTTNIGSFPQTTEIRQARSAFKKGELSAADYEAAMKKEIALVVEEQEKLDLDVLVHGEAERN DMVEYFGELLSGFAFTQYGWVQSYGSRCVKPPIIFGDVSRPEAMTVAWSTYAQSLTKRPMKGMLTGPVTI LQWSFVRNDIPRSTVCKQIALALNDEVLDLEKAGIKVIQIDEPAIREGLPLKRADWDAYLNWAGESFRLS SAGCEDSTQIHTHMCYSEFNDILPAIAAMDADVITIETSRSDMELLTAFGEFQYPNDIGPGVYDIHSPRV PTEAEVEHLLRKAIEVVPVERLWVNPDCGLKTRGWKETLEQLQVMMNVTRKLRAELAK Virmugen A metH mutant, in combination with a siaD mutation, is attenuated in mice and induces significant protection from challenge with wild type N. meningitidis [Ref1804:Li et al., 2004]. NspA from N. meningitidis MC58 Neisseria meningitidis MC58 VO_0010979 902774 15676561 NMB0663 AE002098 NP_273705 1P4T 122586 690297 690821 - outer membrane protein 10.02 17106.9 174 identified by similarity to EGAD:137514; match to protein family HMM PF02462 >NC_003112.2:690297-690821 Neisseria meningitidis MC58 chromosome, complete genome ATCAGAATTTGACGCGCACACCGGCGGACAGTTCGCCGGAACGGACGTTTTTGACAGTGTTGACTTTGCC GATGTAGTTGTAGCGGTAGCCGGCATCCAAATCGACATTCGGGGTAACGGCATAGCTTACGCCCGTCAAT ACGCCGAGGCCGATGGAGGTTTGGCTGAAGCTGTCGCTGCCGCCCAAGTCGACGGAGGCGCGGTTGAGGC TCAAGCGCGCGCCGAGATACGGTTTGACGGGCGATTGGGTGTCGAAGTCGTAAATGGCGGACGCGCCGAT GCTGTAAAGTTTGAAATCGGTGGATGGGGCTTTATAGTTTTTGTAGCGCGTGTAATCGACGGCGAAGCGG AGGTCGTTGATGCGGTAGCCTGCGGAGATGCGCGGGCTGAAGCCTTTGGCAGAACCTAAAGAGCTTGAGG CTTTTGCGTGTGCGGCATCGGCTTGGACGTAAAAGCCGGATGCGCCTTCCGCCAGTGCGGCGGCCGGGAG AGCGAGGGCAATCAGTGTGGCAAGTGCTTTTTTCA >NP_273705.1 outer membrane protein [Neisseria meningitidis MC58] MKKALATLIALALPAAALAEGASGFYVQADAAHAKASSSLGSAKGFSPRISAGYRINDLRFAVDYTRYKN YKAPSTDFKLYSIGASAIYDFDTQSPVKPYLGARLSLNRASVDLGGSDSFSQTSIGLGVLTGVSYAVTPN VDLDAGYRYNYIGKVNTVKNVRSGELSAGVRVKF Protective antigen Protective antigen [Ref859:Martin et al., 1997] NspA-containing outer membrane vesicles conferred protection against otherwise lethal intraperitoneal challenge of mice with N. meningitidis serogroup B, and sera raised against them mediated opsonophagocytosis of meningococcal strains expressing this antigen [Ref1197:O'dwyer et al., 2004]. rfaF Neisseria meningitidis MC58 904029 15677379 NMB1527 AE002098 NP_274534 122586 1577173 1578183 - ADP-heptose:LPS heptosyltransferase II 7.02 35354.86 336 identified by similarity to EGAD:40767; match to protein family HMM PF01075; match to protein family HMM TIGR02195 >gi|77358697:1577173-1578183 Neisseria meningitidis MC58, complete genome ATCATACCGCCTCTTCAACCGCCTGCACAATCTTCTCGGGATACAGCCTGTTGAGGCAGTCGGTATGCCC CAGCGGACATTCCCGCTTAAAACACGGCGAACATTCCAAGTGCAGGCTGACGATTTTCGCCCTATCGCTC AAAGGCGGCGTATGCGTCGGGCTGGAAGAACCGTAAACCGCCACCACCTTCCTGCCCAAAGCTGCCGCCA AATGCATCAATCCGCTGTCGTTACACACGACCGTGTCCGCCAACGACAGCAAATCCATTGCCTGCGACAA ATCGGTTTTGCCGCACAAATTGACACACATACCGTCTGAAAGGCGGTTGATTTCCTCGGCAATTTCATCA TCTTTTTGCGAACCGAACAGCCAAACCTGCCAACCCGCCGCCAGATAATGTTTGCCCAACTCGGCAAAAT GCCTTGTCGGCCAACGCTTTGCCGGCCCGAATTCCGCACCCGGACAAAAAGCCAGAACAGGCTTTCCAAT ATCCAAGCCAAAGGTTTCGACAGAAATTTCCCGCCGCCGTTCATCAATGGAAAACTCGGGGAATCCCGAA TGCCCGTCAAAATCTTCCTGACTCGGATGCGCGAGAGCCGTATATCGATCCACCATCAAAGGCAGACGTT CCTTATCCAGCCTGCGTATATCGTTCAACAGAAAATAACGGCTTTCACCGACATAACCCGTCCTTTTACC GATACCTGTCGCCAGCGCGATGATTGCCGATTTCAAAGAACCGGGCAACACGATAACCTGATCGTATCCG CGCCGCCCCAAATCCCTACCGACCCGCCAACGGCGTTTCAACTCCAACGCACCATGTCCGAACGAATTCT CAAGAATTTCATTCACTTCCGGCATACGCTCGAACACCGCCATCGACCACTTCGGTGCGAACACATCAAT CGTGCAACCGGGGTGAAGTTCCTTCAAACGGCGGAACAAGGGCTGGGTCATCACGCAGTCGCCTATCCAA CTGGGGGAAATAATCAGGATTTTGATGGACA >gi|15677379|ref|NP_274534.1| ADP-heptose:LPS heptosyltransferase II [Neisseria meningitidis MC58] MSIKILIISPSWIGDCVMTQPLFRRLKELHPGCTIDVFAPKWSMAVFERMPEVNEILENSFGHGALELKR RWRVGRDLGRRGYDQVIVLPGSLKSAIIALATGIGKRTGYVGESRYFLLNDIRRLDKERLPLMVDRYTAL AHPSQEDFDGHSGFPEFSIDERRREISVETFGLDIGKPVLAFCPGAEFGPAKRWPTRHFAELGKHYLAAG WQVWLFGSQKDDEIAEEINRLSDGMCVNLCGKTDLSQAMDLLSLADTVVCNDSGLMHLAAALGRKVVAVY GSSSPTHTPPLSDRAKIVSLHLECSPCFKRECPLGHTDCLNRLYPEKIVQAVEEAV Virmugen An rfaF mutant, in combination with a siaD mutation, is attenuated in mice and induces significant protection from challenge with wild type N. meningitidis [Ref1804:Li et al., 2004]. siaD Neisseria meningitidis MC58 903210 15677983 NMB0067 AE002098 NP_273131 122586 76612 77289 - polysialic acid capsule biosynthesis protein SiaD 10.48 25814.56 225 identified by similarity to GP:530041 >gi|77358697:76612-77289 Neisseria meningitidis MC58, complete genome CTTAATCGCCTTGCAGCACATCCCCCTTTCGCCAGGCAAAAAACCGGTTATATTTTTTTGCATTAAATAT TTTTTTAGCATATTCAGGAAAGGGGACATGCAATATGTCAAAATGATCTATATATCCTTTAATATTAAGA TTATTTCCAATCAAATAACGTTCTAATTTTGTTGGATGATATGAAAATGATTCTAATAAAGGAGCATATG TTCCAGTCCCTTCATCAATTAAATGAGTCGTAATATTCTTTTTTTTTGCAATACTAATCAGATAGGAGTA GTGGCCTGTAAAAGACAGCATATAGAGATGAGCAGGCTGTATAATATTAAGGATTTTTTTGTAACTTCTA TAAATATAAAGTAATTTTTTAGGAGTTATATTATTAGGGCTTCTAGGAAGCTCAAATAGATAAATAGATT CAAATAGATTCTTGTTAGCTGATTGATGAACTAACTTAGGCATTTTTAAGTTTTTAGAAGTATATAAAAT TACTAGTAAATTATTGGTTAATTTTTGTATTTTAATTAGGCTTTGGACTTGGTTAAGCTGACCTAAATTA GATATGACAAATAAATTGTTACGTGGGGGGGTAAGATAAAATGGAGATGTTGTCAACCACATTGAATCTT GAAAAAACTTTTTAGGCTGAAAAAGAGCTTTTTTTATTTTCTTTAGCA >gi|15677983|ref|NP_273131.1| polysialic acid capsule biosynthesis protein SiaD [Neisseria meningitidis MC58] MLKKIKKALFQPKKFFQDSMWLTTSPFYLTPPRNNLFVISNLGQLNQVQSLIKIQKLTNNLLVILYTSKN LKMPKLVHQSANKNLFESIYLFELPRSPNNITPKKLLYIYRSYKKILNIIQPAHLYMLSFTGHYSYLISI AKKKNITTHLIDEGTGTYAPLLESFSYHPTKLERYLIGNNLNIKGYIDHFDILHVPFPEYAKKIFNAKKY NRFFAWRKGDVLQGD Virmugen A siaD mutant, in combination with either a metH or rfaF mutation, is attenuated in mice and induces protection from challenge with wild type N. meningitidis [Ref1804:Li et al., 2004]. tbp2 Neisseria meningitidis VO_0011182 NP_273507 CDD:307461 122586 ? transferrin-binding protein B 5.85 74897.85 797 Transferrin binding protein-like solute binding protein; pfam01298 >NP_273507.1 transferrin-binding protein B [Neisseria meningitidis MC58] MNNPLVNQAAMVLPVFLLSACLGGGGSFDLDSVDTEAPRPAPKYQDVFSEKPQAQKDQGGYGFAMRLKRR NWYPQAKEDEVKLDESDWEATGLPDEPKELPKRQKSVIEKVETDSDNNIYSSPYLKPSNHQNGNTGNGIN QPKNQAKDYENFKYVYSGWFYKHAKREFNLKVEPKSAKNGDDGYIFYHGKEPSRQLPASGKITYKGVWHF ATDTKKGQKFREIIQPSKSQGDRYSGFSGDDGEEYSNKNKSTLTDGQEGYGFTSNLEVDFHNKKLTGKLI RNNANTDNNQATTTQYYSLEAQVTGNRFNGKATATDKPQQNSETKEHPFVSDSSSLSGGFFGPQGEELGF RFLSDDQKVAVVGSAKTKDKPANGNTAAASGGTDAAASNGAAGTSSENGKLTTVLDAVELKLGDKEVQKL DNFSNAAQLVVDGIMIPLLPEASESGNNQANQGTNGGTAFTRKFDHTPESDKKDAQAGTQTNGAQTASNT AGDTNGKTKTYEVEVCCSNLNYLKYGMLTRKNSKSAMQAGESSSQADAKTEQVEQSMFLQGERTDEKEIP SEQNIVYRGSWYGYIANDKSTSWSGNASNATSGNRAEFTVNFADKKITGTLTADNRQEATFTIDGNIKDN GFEGTAKTAESGFDLDQSNTTRTPKAYITDAKVQGGFYGPKAEELGGWFAYPGDKQTKNATNASGNSSAT VVFGAKRQQPVR Protective antigen Mice immunized with purified Tbp2 survived a lethal challenge to a similar degree as animals immunized with the Tbp1-Tbp2 complex, demonstrating that Tbp2 played an important role in the protective activity observed with the complex, eliciting antibodies that are not only bactericidal but also inhibitory for meningococcal growth [Ref1195:Lissolo et al., 1995]. tbpA Neisseria meningitidis K454 VO_0012380 8926211 CDD:273799 CDD:238657 487 ? transferrin-binding protein A 9.8 96910.19 997 TbpA >AAF81744.1 transferrin-binding protein A [Neisseria meningitidis] MQQQHLFRFNILCLSLMTALPAYAENVQAGQAQEKQLDTIQVKAKKQKTRRDNEVTGLGKLVKSSDTLSK EQVLNIRDLTRYDPGIAVVEQGRGASSGYSIRGMDKNRVSLTVDGVSQIQSYTAQAALGGTRTAGSSGAI NEIEYENVKAVEISKGSNSVEQGSGALAGSVAFQTKTADDVIGEGRQWGIQSKTAYSGKNRGLTQSIALA GRIGGAEALLIHTGRRAGEIRAHEDAGRGVQSFNRLVPVEDSSNYAYFIVKEECKNGSYETCKANPKKDV VGKDERQTVSTRDYTGPNRFLADPLSYESRSWLFRPGFRFENKRHYIGGILEHTQQTFDTRDMTVPAFLT KAVFDANKKQAGSLPGNGKYAGNHKYGGLFTNGENGALVGAEYGTGVFYDETHTKSRYGLEYVYTNADKD TWADYARLSYDRQGVGLDNHFQQTHCSADGSDKYCRPSADKPFSYYKSDRVIYGESHRLLQAAFKKSFDT AKIRHNLSVNLGFDRFGSNLRHQDYYYQHANRAYSSNTPPQNNGKKISPNGSETSPYWVTIGRGNVVTGQ ICRLGNNTYTDCTPRSINGKSYYAAVRDNVRLGRWADVGAGLRYDYRSTHSDDGSVSTGTHRTLSWNAGI VLKPTDWLDLTYRTSTGFRLPSFAEMYGWRAGVQSKAVKIDPEKSFNKEAGIVFKGDFGNLEASWFNNAY RDLIVRGYEAQIKDGKEEAKGDPAYLNAQSARITGINILGKIDWNGVWDKLPEGWYSTFAYNRVRVRDIK KRADRTDIQSHLFDAIQPSRYVVGLGYDQPEGKWGVNGMLTYSKAKEITELLGSRALLNGNSRNTKATAR RTRPWYIVDVSGYYTVKKHFTLRAGVYNLLNYRYVTWENVRQTAGGAVNQHKNVGVYNRYAAPGRNYTFS LEMKF Protective antigen Recombinant TbpA protein was used in a mouse intraperitoneal-infection model to determine their ability to protect against meningococcal infection and to induce cross-reactive and bactericidal antibodies. TbpA was found to afford protection against meningococcal challenge when administered as the sole immunogen [Ref1488:West et al., 2001]. 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