Leishmania donovani 5661 The intracellular amastigote form multiplies in macrophages and produces a reticuloendothelial hyperplasia grossly affecting the spleen and liver, with other lymphoid tissues being involved as well, resulting in severe hepatosplenomegaly, which usually is fatal if untreated (WD: Leishmania donovani). Visceral leishmaniasis A Strong Th1 response of cell mediated immunity is necessary for protection against L. donovani (Mizbani et al., 2009). Vector sand flies are infected by biting infected humans or animals. Animal reservoirs vary with the Leishmania sp and location and include canines, rodents, and other animals. In the Indian subcontinent, humans are the reservoir for L. donovani (Merck Manual: Leishmaniasis). Leishmania donovani is a species that is the causal agent of visceral leishmaniasis in Mediterranean and adjacent countries, the south central section of western Asia, eastern India, northern China, Kenya, Ethiopia, and the Sudan; also found in Brazil, Argentina, Colombia, and Venezuela; in the Old World, it is transmitted by various species of Phlebotomus; New World vectors are species of Lutzomyia; dogs and other carnivores are known as reservoir hosts in some areas (WD: Leishmania donovani). 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 ChAd63-KH VO_0003961 Recombinant vector vaccine Clinical trial adenovirus 63 Intramuscular injection (i.m.) A recombinant vector vaccine for Leishmania donovani that uses an adenovirus 63 viral vector and kH protein (Osman et al., 2017). Intramuscular injection (i.m.) KH, a self-cleaving polyprotein comprising L. donovani HASPB and KMP-11 Proteins (Osman et al., 2017) L. donovani Beta-tubulin Protein Vaccine VO_0004023 Subunit vaccine Research Intraperitoneal injection (i.p.) Cationic liposomes (Bhowmick and Ali, 2009). Intraperitoneal injection (i.p.) four polypeptides 91(LD91), 72 (LD72), 51(LD51) and 31 (LD31)-kDa (Bhowmick and Ali, 2009) Recombinant protein preparation BALB/c Mice were immunized by intraperitoneal injections of 2.5 µg purified proteins in PBS or incorporated in liposome in a total volume of 200 µl. Animals receiving PBS or empty liposomes served as controls. Mice were boosted two times at 2-week intervals (Bhowmick and Ali, 2009). Results demonstrated that liposomal LD51 (beta-tubulin) reduced parasite burden by 72%-75% (Bhowmick and Ali, 2009). Ten days after the final immunization the mice were challenged with 2.5×10^7 freshly transformed stationary-phase promastigotes in 200 µl PBS injected intravenously via the tail vein (Bhowmick and Ali, 2009). L. donovani DNA Vaccine encoding KMP-11 VO_0011530 DNA vaccine Research pCMV-LIC [Ref1167:Bhaumik et al., 2009]. Subcutaneous injection Subcutaneous injection KNP-11(Bhaumik et al., 2009) DNA vaccine construction KMP-11was cloned into a pCMV-LIC vector for DNA vaccine candidate in mice (Bhaumik et al., 2009). KMP-11 DNA immunization alone effectively caused a significant increase in frequency of both IFN-γ producing CD4+ T and CD8+ T cells in mice challenged with either LM or LD (Bhaumik et al., 2009). BALB/c BALB/c mice were either immunized with KMP-11 containing pCMV-LIC mammalian expression vector (pCMV-LIC KMP-11) or with blank-vector construct not harboring KMP-11 gene (pCMV-LIC). rmIL-12 (1 μg/injection) was used as an adjuvant and injected through s.c. route. 7 and 15 days before parasite challenge with LD or LM, 100 μg of endotoxin-free plasmid DNA construct (pCMV-LIC, and pCMV-LIC KMP-11) dissolved in saline and injected i.m. in the hind leg thigh muscle was used for immunization of BALB/c mice using 28-gauge needle (Bhaumik et al., 2009). KMP-11 DNA vaccination alone in an experimental BALB/c mice model showed significant potential in terms of resolution of splenic and hepatic parasite burden against virulent LD challenge. KMP-11 DNA immunization significantly protects against L. donovani infection (Bhaumik et al., 2009). 6-weeks-old BALB/c mice were injected with 2 × 10^6 LD second-passage promastigotes suspended in saline through intracardiac route and 2 × 10^6 LM second-passage promastigotes through subcutaneous route in the hind footpad using a 28-gauge needle (Bhaumik et al., 2009). L. donovani DNA Vaccine encoding NH36 Protein VO_0011542 DNA vaccine Research VR1012 [Ref1171:Aguilar-Be et al., 2005] Intramuscular injection (i.m.) Intramuscular injection (i.m.) NH36 (Aguilar-Be et al., 2005) DNA vaccine construction BALB/c Mice were immunized via intramuscular with 100 μg of VR1012-NH36 plasmid DNA in 100 μl of saline solution and boosted 2 weeks later by a second injection. Control groups included the empty VR1012 vector and saline solution (Aguilar-Be et al., 2005). Experimental infection of immunized BALB/c mice demonstrated that the VR1012-NH36 DNA vaccine derived from the nucleoside hydrolase gene (NH) of L. donovani induced an 88% reduction in L. chagasi parasite load and a 65% reduction in L. mexicana lesion size (Aguilar-Be et al., 2005). At 2 weeks after immunization, animals were challenged by intravenous injection of 2 × 10^8 amastigotes of L. chagasi (MHOM/BR/72/BH46), another group of mice were challenged 2 weeks after the last immunization with 106 stationary-phase promastigotes of L. mexicana (MNYC/BZ/62/379) by s.c. injection in the hind footpad (Aguilar-Be et al., 2005). L. donovani gp63 Protein Vaccine VO_0011532 Subunit vaccine Research Intraperitoneal injection (i.p.) Cationic distearoyl phosphatidylcholine (DSPC) liposomes (Bhowmick et al., 2008). Intraperitoneal injection (i.p.) gp63 Recombinant protein preparation BALB/c BALB/c mice were immunized by three intraperitoneal (i.p.) injections at 2-week intervals with graded doses (0.6 to 10 μg) or 2.5 μg of gp63 free in phosphate-buffered saline (PBS) or entrapped in liposomes (200 μl). Animals receiving only PBS or empty liposomes served as controls (Bhowmick et al., 2008). gp63 used without adjuvant elicited partial protection but in association with liposomes exhibited marked resistance in both the livers and spleens of the mice challenged 10 days after the last vaccination (Bhowmick et al., 2008). At 10 days or 12 weeks postimmunization, groups of mice were either sacrificed for immunological assays or challenged intravenously with 2.5 × 10^7 freshly transformed L. donovani promastigotes (Bhowmick et al., 2008). L. donovani GRP-78 Protein Vaccine VO_0004022 Subunit vaccine Research Subcutaneous injection recombinant IL-12 (Nagill and Kaur, 2010). Subcutaneous injection GRP-78 (Nagill and Kaur, 2010) Recombinant protein preparation BALB/c Ten microgram of 78 kDa antigen along with different concentrations of adjuvants was used to immunize animals. Subcutaneous route was used for immunization of mice in all the groups. Twenty-five BALB/c mice were used for each immunization group and the control group (immunized with PBS only).The animals who received only PBS as vaccine candidate served as controls. Two booster doses with the same respective vaccine combination were given to all immunized groups at an interval of 2 weeks each (Nagill and Kaur, 2010). Maximum protection was conferred by 78 kDa antigen + rIL-12 vaccine (with parasite load reduction of 71–94.8% on 30–90 p.c.d.) (Nagill and Kaur, 2010) Two weeks after last booster dose, mice of control and immunized groups were challenged with 1 × 10^7 promastigotes (Nagill and Kaur, 2010). L. donovani HASPB1 Protein Vaccine VO_0004067 Subunit vaccine Research Subcutaneous injection Subcutaneous injection Recombinant hydrophilic acylated surface protein B1 (HASPB1) (Stäger et al., 2000). Recombinant protein preparation BALB/c In the first two vaccination experiments, BALB/c mice received s.c. immunization with either 1) 10 µg rHASPB1 with 1 µg murine rIL-12; 2) 10 µg rHASPB1 in saline; 3) 10 µg SLA plus 1 µg rmIL-12; 4) 1 µg rmIL-12; and 5) saline. Three weeks later, mice were boosted with the same schedule, but the IL-12 dose was reduced to 0.5 µg. After an additional 3 wk, a final boost was given omitting IL-12. In the third vaccination experiment, mice were immunized three times at 3-wk intervals with 10 µg rHASPB1 or OVA (Sigma) (Stäger et al., 2000). rHASPB1 provided significant protection against challenge with L. donovani (Stäger et al., 2000). All mice were challenged 3 wk after the last boost with 2 x 10^7 amastigotes, given i.v. in the lateral tail vein (Stäger et al., 2000). L. donovani Hsp70 Protein Vaccine VO_0004033 Subunit vaccine Research Liposomes Intraperitoneal injection (i.p.) Intraperitoneal injection (i.p.) LD72 (Hsp70) protein Recombinant protein preparation BALB/c Mice were immunized by intraperitoneal injections of 2.5 µg purified proteins in PBS or incorporated in liposome in a total volume of 200 µl. Animals receiving PBS or empty liposomes served as controls. Mice were boosted two times at 2-week intervals (Bhowmick and Ali, 2009). Mice immunized with liposomal LD72 (Hsp70) had a reduced parasite burden of 65%-67% (Bhowmick and Ali, 2009). Ten days after the final immunization rest of the mice were challenged with 2.5×10^7 freshly transformed stationary-phase promastigotes in 200 µl PBS injected intravenously via the tail vein (Bhowmick and Ali, 2009). L. donovani LD31 Protein Vaccine VO_0004179 Subunit vaccine Research Intraperitoneal injection (i.p.) Cationic liposomes (Bhowmick and Ali, 2009). Intraperitoneal injection (i.p.) Recombinant protein preparation BALB/c Mice were immunized by intraperitoneal injections of 2.5 µg purified proteins in PBS or incorporated in liposome in a total volume of 200 µl. Animals receiving PBS or empty liposomes served as controls. Mice were boosted two times at 2-week intervals (Bhowmick and Ali, 2009). Liposomal LD31 (ATP synthase alpha chain) reduced parasite burden by 74%-77% (Bhowmick and Ali, 2009). Ten days after the final immunization the mice were challenged with 2.5×10^7 freshly transformed stationary-phase promastigotes in 200 µl PBS injected intravenously via the tail vein (Bhowmick and Ali, 2009). L. donovani ORFF Protein Vaccine VO_0011539 Subunit vaccine Research Intramuscular injection (i.m.) An expression plasmid encoding both p35 and p40 subunits of IL-12 was used as an adjuvant (Tewary et al., 2006). Intramuscular injection (i.m.) Recombinant protein preparation BALB/c Injections were given at midpoint of left thigh muscle. For the vaccination studies, cell proliferation, cytokine production and antibody response BALB/c mice were immunized intramuscularly with either alum alone diluted in phosphate buffered saline (PBS) final volume 100 or 50 μg of rORFF adsorbed on alum or 100 μg of IL-12 plasmid DNA diluted in PBS or 50 μg of rORFF adsorbed on alum in combination with IL-12 DNA. Three weeks later mice were immunized with the same schedule (Tewary et al., 2006). An expression plasmid encoding both p35 and p40 subunits of IL-12 when co-administered with a recombinant open-reading frame (rORFF) gene from the LD1 locus of Leishmania donovani induces significant protection with around 82% protection in both liver and spleen of BALB/c mice when challenged with L. donovani (Tewary et al., 2006). 1 × 10^8 stationary phase promastigotes of L. donovani were injected intravenously via the tail vein in 100 μl of PBS per mouse (Tewary et al., 2006). L. donovani Recombinant LdγGCS in NIV system Vaccine VO_0004241 Subunit vaccine Research Intravenous injection (i.v.) Intravenous injection (i.v.) Recombinant Leishmania donovani gamma-glutamyl cysteine synthetase protein (LdγGCS) (Henriquez et al., 2010). BALB/c The day of infection was day 0 so that vaccination occurred pre-infection on day −28 and day −14. Animals (n  =  5/treatment) were immunized with either LPS (10 ng/ml equivalent to 5 EU/ml, 1 ng/dose), LdγGCS (2 or 50 µg, used as prepared or processed to remove endotoxin), or LdγGCS incorporated into NIV (50 µg) on days −28 and −14 (Henriquez et al., 2010). Incorporating LdγGCS into a NIV formulation was more effective than immunization with LdγGCS alone based on its ability to induce specific antibody pre- and post-infection. However, the vesicular formulation gave a similar level of protection as immunization with LdγGCS alone (Henriquez et al., 2010). On day 0 immunized mice and a control group (n  =  4–10/treatment) were infected by intravenous injection (tail vein, no anaesthetic) with 1–2 × 10^7 L. donovani strain 200016 amastigotes harvested from the spleen of an infected hamster (Henriquez et al., 2010). LEISH-F1+MPL-SE vaccine VO_0004266 Subunit vaccine Clinical trial subcutaneous injection subcutaneous injection Recombinant Leishmania polyprotein LEISH-F1 (formerly known as Leish-111f) antigen. The antigen component of the vaccine includes three proteins derived from L. major and conserved across various Leishmania species, including L. donovani; L. chagasi, which causes New World VL; and L. braziliensis, which causes both CL and mucosal leishmaniasis (ML) in the New World. The three proteins are: Leishmania elongation initiation factor (LeIF), thiol-specific antioxidant (TSA), and Leishmania major stress-inducible protein 1 (LmSTI1) (Chakravarty et al., 2011). There were statistically significant increases in median cytokine concentrations at day 84 compared to day 0 for all measured cytokines except IL-4 in the DAT-positives and IL-10 in both DAT-negatives and DAT-positives, although in some cases the differences were quite small (Chakravarty et al., 2011). The subjects in this trial were healthy male and female adults ≥18 years and <55 years of age from the village near Varanasi that had experienced an outbreak of VL approximately 15 years prior to the start of the trial. Eligible subjects were enrolled into the trial in three sequential cohorts (Fig. 1a). The vaccine consisted of LEISH-F1 antigen (5 μg in Cohort 1, 10 μg in Cohort 2, and 20 μg in Cohort 3) + MPL-SE adjuvant (25 μg), and was administered subcutaneously in the upper arm in a volume of 0.5 mL on days 0, 28, and 56. Subjects were followed through day 168 (Chakravarty et al., 2011). Malaise was the predominant solicited systemic reaction, followed by myalgia, pyrexia, and headache. All local injection-site and systemic reactions were of mild or moderate severity (Chakravarty et al., 2011). The LEISH-F1 + MPL-SE vaccine was safe and well-tolerated in this population of DAT-negative and DAT-positive subjects (Chakravarty et al., 2011). There were statistically significant increases in median cytokine concentrations at day 84 compared to day 0 for all measured cytokines except IL-4 in the DAT-positives and IL-10 in both DAT-negatives and DAT-positives, although in some cases the differences were quite small (Chakravarty et al., 2011). The subjects in this trial were healthy male and female adults ≥18 years and <55 years of age from the village near Varanasi that had experienced an outbreak of VL approximately 15 years prior to the start of the trial. Eligible subjects were enrolled into the trial in three sequential cohorts (Fig. 1a). The vaccine consisted of LEISH-F1 antigen (5 μg in Cohort 1, 10 μg in Cohort 2, and 20 μg in Cohort 3) + MPL-SE adjuvant (25 μg), and was administered subcutaneously in the upper arm in a volume of 0.5 mL on days 0, 28, and 56. Subjects were followed through day 168 (Chakravarty et al., 2011). Malaise was the predominant solicited systemic reaction, followed by myalgia, pyrexia, and headache. All local injection-site and systemic reactions were of mild or moderate severity (Chakravarty et al., 2011). The LEISH-F1 + MPL-SE vaccine was safe and well-tolerated in this population of DAT-negative and DAT-positive subjects (Chakravarty et al., 2011). Leishmania donovani cen1 mutant vaccine VO_0003005 Live, attenuated vaccine Research Intravenous injection (i.v.) Intravenous injection (i.v.) Gene mutation This cen1 mutant is from Leishmania donovani (Selvapandiyan et al., 2009). A cen1 mutant is attenuated in hamsters (Selvapandiyan et al., 2009). A cen1 mutant induces significant protection in hamsters from challenge with wild type L. donovani (Selvapandiyan et al., 2009). A cen1 mutant is attenuated in mice (Selvapandiyan et al., 2009). A cen1 mutant induces significant protection in mice from challenge with wild type L. donovani (Selvapandiyan et al., 2009). The results thus indicate an increased IFN-γ secretion coinciding with reduced IL-10 production among the immunized mice. In the restimulated CD4+ T cells from the spleen, the IFN-γ/IL-10 ratio was significantly higher in the immunized mice both at the time of challenge (5 weeks after immunization) and after challenge (5 weeks after immunization plus 10 weeks after challenge) compared with either naive or naive-challenged controls. We also observed an absolute requirement for IFN-γ in LdCen1−/−-induced immunity. IFN-γ knockout mice immunized with LdCen1−/− for 5 wk followed by challenge were not protected (Selvapandiyan et al., 2009). The number of T cells producing TNF-alpha increased significantly as compared to naive mice 5 weeks after immunization in CD8+ cells as well as 5 weeks after immunization plus 10 weeks after challenge in both CD4+ and CD8+ cells (Selvapandiyan et al., 2009). The number of T cells producing IL-2 increased significantly as compared to naive mice 5 weeks after immunization in CD4+ and CD8+ cells as well as 5 weeks after immunization plus 10 weeks after challenge in both CD4+ and CD8+ cells (Selvapandiyan et al., 2009). Sera from BALB/c mice taken 10 wk post challenge after 5, 12, or 16 immunization weeks were measured for Leishmania-specific IgG2a responses. Results indicated a significantly higher level of IgG2a populations in the immune-challenged groups compared with the naive challenged groups (Selvapandiyan et al., 2009). Leishmania vaccine using recombinant L. tarentolae strain expressing A2 antigen VO_0004180 Recombinant vector vaccine Research Leishmania tarentolae, a non-pathogenic member of the genus Leishmania [Ref1165:Mizbani et al., 2009]. Intraperitoneal injection (i.p.) Intraperitoneal injection (i.p.) mouse Recombinant protein preparation BALB/c In the case of i.p. immunization, total number of 5 × 10^6 stationary-phase promastigotes were used. Mice were immunized with L. tarentolae expressing the GFP only as a control and another group were immunized with recombinant L. tarentolae-A2 (Mizbani et al., 2009). Study results show that a single intraperitoneal administration of the A2-recombinant L. tarentolae strain expressing the Leishmania donovani A2 antigen protects BALB/c mice against L. infantum challenge and that protective immunity is associated with high levels of IFN-gamma production prior and after challenge (Mizbani et al., 2009). Six weeks after immunization, animals were challenged with 10^7 virulent stationary-phase L. infantum promastigotes through the lateral tail vein (Mizbani et al., 2009). Leishmune Leishmune Fort Dodge VO_0001200 Inactivated or "killed" vaccine Licensed Intramuscular injection (i.m.) Native fucose-mannose-ligand antigen complex(Borja-Cabrera et al., 2002) Intramuscular injection (i.m.) licensed Visceral leishmaniasis human vaccine Generic Unknown VO_0001142 Live, attenuated vaccine Licensed A generic representation of vaccines developed to prevent visceral leishmaniasis in humans, most commonly utilizing live, attenuated Leishmania parasites to stimulate protective immunity. These vaccines aim to mimic natural infection while minimizing pathogenicity. pVAX-P1 DNA vaccine VO_0004272 DNA vaccine Research pVAX1 [Ref2053:Arora et al., 2011] Intramuscular injection (i.m.) pVAX-P1 DNA vaccine, given in prime-boost mode is protective against L. donovani (Arora et al., 2011). Intramuscular injection (i.m.) P1 gene of Leishmania donovani (Arora et al., 2011). DNA vaccine construction The purified full-length ORF cloned non-directionally in pGEMT-Easy vector was digested out and then directionally sub-cloned in pVAX1 vector (Invitrogen, USA). The purified plasmid DNA containing full-length ORF was confirmed by DNA sequencing also. The plasmid DNA was made endotoxin-free by using Endofree Plasmid DNA Mega Purification Kit (Qiagen, Hilden, Germany) according to the manufacturer’s instructions. The endotoxin free plasmid DNA (termed pVAX-P1) was used for the immunization of animals as DNA vaccine (Arora et al., 2011). Syrian golden Six weeks old Syrian golden hamsters (Mesocricetus auratus) were immunized in the following groups, with 6 hamsters per group. Group I: Naïve animals (Unimmunized – uninfected) were given PBS only and not challenged, group II: Animals were immunized with recombinant protein vaccine, rLdP1 (50 μg) along with Complete Freund’s adjuvant and two booster doses of same amount of antigen given with Incomplete Freund’s adjuvant, group III: Hamsters immunized with plasmid DNA vaccine alone, pVAX1-P1 single dose, group IV: Hamsters immunized with pVAX-P1 and given a prime-boost dose after 15 days, group V: Hamsters immunized with pVAX1-vector only and group VI: Unimmunized – were given PBS only (Arora et al., 2011). Prime-boost immunization with pVAX-21 DNA vaccine resisted the increase in spleen parasite burden by 75.68% (Arora et al., 2011). All the animals except group I, were challenged with 1 × 10^7 promastigotes (from late log-phase axenic cultures) intracardially (i.c.) on day 28. The hamsters were observed for 6–8 weeks post challenge (p.c.). At the end of 10 weeks post infection, the surviving animals were euthanized and parasitological and immunological parameters were studied (Arora et al., 2011). SL3261-L. donovani VO_0004672 Recombinant vector vaccine Research Intramuscular injection (i.m.) Five chosen antigens were differentially expressed on the surface or in the cytosol of Salmonella typhimurium SL3261. A two-step procedure was developed to select optimal Salmonella vaccine strains for each antigen, based on bacterial fitness and antigen expression levels (Schroeder et al., 2011). Intramuscular injection (i.m.) Recombinant vector construction The sequence encoding cholera toxin B subunit signal peptide was followed by SpeI/BglII sites for in frame directional cloning of ORF of interest fused with downstream sequences coding for a hemagglutinin epitope (HA)-tag and the transporter domain of AIDA (Schroeder et al., 2011) Mice were vaccinated with a single dose of Salmonella vaccine strains, the carrier control SL3261 or treated with PBS (Schroeder et al., 2011). VO_0003057 The vaccine strains of Salmonella expressing the novel Leishmania antigens LinJ08.1190 and LinJ23.0410 significantly reduced visceralisation of L. major and enhanced systemic resistance against L. donovani in susceptible BALB/c mice. The results show that Salmonella are valid vaccine carriers for inducing resistance against visceral leishmaniasis but that their use may not be suitable for all antigens (Schroeder et al., 2011). Mice were subsequently challenged with 2×10^6 late-stationary phase L. major promastigotes into the left hind footpad (Schroeder et al., 2011). A2 Leishmania donovani VO_0011153 30385439 5671 ? stage-specific S antigen-like protein 4.19 9285.64 194 zymodeme MON-29 >AAP21105.1 stage-specific S antigen-like protein [Leishmania infantum] MKIRSVRPLVVLLVCVAAVLALSASAEPHKAAVDAGPLSVDVGPLSVDVGPLSVGPQSVGPLSVGPQSVD PLSVDVGPLSVGPQSVGPLSVDVGPLSVGPQSVGPLSVGLQAVDVSPVS Protective antigen Study results show that a single intraperitoneal administration of the A2-recombinant L. tarentolae strain expressing the Leishmania donovani A2 antigen protects BALB/c mice against L. infantum challenge and that protective immunity is associated with high levels of IFN-gamma production prior and after challenge [Ref1165:Mizbani et al., 2009]. Beta-tubulin Leishmania donovani VO_0011155 262233287 CDD:276956 CDD:240228 5661 ? beta tubulin 6.31 37694.97 416 The beta-tubulin family; cd02187 >ACY38664.1 beta tubulin, partial [Leishmania donovani] ESAGGRYVPRAVLMDLEPGTMDSVRAGPYGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRK EAESCDCLQGFQLSHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVIPSPRVSDTVVEPYNTTLSVHQL VENSDESMCIDNEALYDICFRTLKLTTPTFGDLNHLVAAVMSGVTCCLRFPGQLNSDLRKLAVNLVPFPR LHFFMMGFAPLTSRGSHQYPGLSVAELTQQMFDAKNMMQAADPRHGRYLTASALFRGRMSTKEVDEQMLN VQNKNSSYFIEWIPNNIKSSICDIPPKGLKMSVTFIGNNTCIQEMFRRVGEQFTGMFRRKACLHWYTGEG MDE Protective antigen Study compared the vaccine efficacy of various L. donovani antigens encapsulated in cationic liposomes in BALB/c mice against challenge infection with L. donovani. Results demonstrated that liposomal LD51 (beta-tubulin) reduced parasite burden by 72%-75% [Ref1166:Bhowmick and Ali, 2009]. cen1 15488542 CDD:185503 CDD:28933 5661 ? centrin 149 centrin; Provisional >gi|15488542|gb|AAL01153.1|AF406767_1 centrin [Leishmania donovani] MAALTDEQIREAFNLFDADGSGAIDAEEMALAMKGLGFGDLSRDEVERIIRSMHTDSNGLVAYGEFEAMV KSRMAQKDSPEEILKAFQLFDLDKKGKISFANLKEVAKLLGENPGDDVLKEMIAEADEDGDGEVSFEEFK SVMLHMRGK Virmugen A cen1 mutant is attenuated in mice and hamsters and induces significant protection from challenge with wild type L. donovani [Ref1775:Selvapandiyan et al., 2009]. F1-ATPase Leishmania donovani VO_0011154 722242 CDD:304359 CDD:238540 CDD:278722 5661 ? F1-ATPase beta subunit 4.18 20953.9 292 promastigotes of Leishmania donovani Sudan 1S maintained in liquid culture as a suspension >AAA73465.1 F1-ATPase beta subunit, partial (mitochondrion) [Leishmania donovani] KVALVYGQMNEPPGARAGVAESAVTMAEYFRDVEGQNVLLFIDNIFRFTQANSEVSALLGRIPAAVGYQP TLAEDLGMLQERITSTTKGSITSVQAVYVPADDITDPAPATTFSHLDATTVLDRAVAESGIYPAVNPLEC ASRIMDPDVIDVDHYNVAQDIVQMLTKYKELQDIIAVLGIDELSEEDKVVVDRARKVTRFLSQPFQ Protective antigen Study compared the vaccine efficacy of various L. donovani antigens encapsulated in cationic liposomes in BALB/c mice against challenge infection with L. donovani. Results demonstrated that liposomal LD31 (ATP synthase alpha chain) reduced parasite burden by 74%-77% [Ref1166:Bhowmick and Ali, 2009]. GRP-78 Leishmania donovani VO_0011152 13386966 16797868 CDD:240227 CDD:212681 5661 ? glucose-regulated protein 78 4.92 63125.03 710 heat shock 70 kDa protein; Provisional >AAL29192.1 glucose-regulated protein 78, partial [Leishmania donovani] GKVEAPCVGVDLGTTYSVAGVWQKGEVHIVTNEMGNRITPSVVAFTDAERLVGDGAKNQLPQNPENTIYA IKRLIGRKYVDPTVQNDKKLLSYHIVADKTGKPLVQVTVKGQQKRFTPEEVSAMVLQKMKEISETFLGEK VKNAVVTVPAYFNDAQRQATKDSGKIAGLNVVRIINEPTAAAIAYGLNKAGEKNILVFDLGGGTFDVSLA DNRRGFFEVVATNGDTHLGGEDFDNNMMKFFVDGLKRKQNVDISNDQKALARLRKACEAAKRQLSSHPEA RVEVDSLVEGYDFSEKITRAKFEELNMALFKNTLVPVQKVLEDAKLKKSDIDEIVLVGGSTRIPKVQQLI KDFFSGKEPNKGINPDEAVAYGAAVQAAVLTGESEVGGKVVLVDVIPLSLGIETVGGVMTKLIERNTQIP TKKSQIFSTYQDNQPSVLIQVFEGERGMTKDNRLLGKFDLSGIPPAPRGVPQIEVAFDVDENSILQVTAS DKSSGKREEITITNDKGRLSEEEIERMVREAAEFEDEDRKVRERVEAKNSLESIAYSLRNQINDKDKLGD KLAADDKKAIEEAVKDALDFVDENPNADREEFEAARTKLQSVTNPIIQKVYQGTAGSGAEEADAMDDL Protective antigen BALB/c mice were immunized with a vaccine expressing the 78kDa (GRP-78) antigen of Leishmania donovani. Challenge infection was given intracardially after 2 weeks of second booster. A significant decrease in parasite burden was seen in vaccinees over the infected controls on all post challenge days and was found that maximum protection was provided by 78kDa+rIL-12 vaccine. It was highly immunogenic as depicted by the reduction in parasite load (71-94.8%) [Ref1164:Nagill and Kaur, 2010]. HASPB1 Leishmania donovani VO_0011162 51847753 CDD:273344 5661 ? cell surface protein B1 4.46 15792.04 217 K+-dependent Na+/Ca+ exchanger; TIGR00927 >AAU10514.1 cell surface protein B1, partial [Leishmania donovani] PKEDGHTQKNDGDGPKEDGHTQKNDGDGPKEDGHTQKNDGDGPKEDGHTQKNDGDGPKEDGHTQKNDGDG PKEDGHTQKNDGDGPKEDGHTQKNDGDGPKEDGHTQKNDGDGPKEDGHTQKNDGDAPKEDGRTQRNDGDG PKEDGH Protective antigen Study demonstrated for the first time that a recombinant stage-specific hydrophilic surface protein of Leishmania donovani, recombinant hydrophilic acylated surface protein B1 (HASPB1), is able to confer protection against experimental challenge with L. donovani in BALB/c mice [Ref1172:Stäger et al., 2000]. hsp70 Leishmania donovani VO_0011156 281426606 CDD:302596 GOA:D2EAU9 InterPro:IPR001023 InterPro:IPR013126 InterPro:IPR018181 UniProtKB/TrEMBL:D2EAU9 5661 ? heat shock protein 70 5.03 47979.15 532 Nucleotide-Binding Domain of the sugar kinase/HSP70/actin superfamily; cl17037 >CAZ04896.1 heat shock protein 70, partial [Leishmania donovani] DSQRQATKDAGTIAGLEVLRIINEPTAAAIAYGLDKGDDGKERNVLIFDLGGGTFDVTLLTIDGGIFEVK ATNGDTHLGGEDFDNRLVTFFTEEFKRKNKGKNLASSHRALRRLRTACERAKRTLSSATQATIEIDALFE NVDFQATITRARFEELCGDLFRSTIQPVERVLQDAKMDKRSVHDVVLVGGSTRIPKVQSLVSDFFGGKEL NKSINPDEAVAYGAAVQAFILTGGKSKQTEGLLLLDVTPLTLGIETAGGVMTALIKRNTTIPTKKSQIFS TYADNQPGVHIQVFEGERAMTKDCHLLGTFDLSGIPPAPRGVPQIEVTFDLDANGILNVSAEEKGTGKRN QITITNDKGRLSKDEIERMVNDAMKYEADDRAQRDRVEAKNGLENYAYSMKNTLGDSNVSGKLDDSDKAT LNKEIDVTLEWLSSNQEATKEEYEHKQKELESVCNPIMT Protective antigen Study compared the vaccine efficacy of various L. donovani antigens encapsulated in cationic liposomes in BALB/c mice against challenge infection with L. donovani. Results demonstrated that liposomal LD72 (Hsp70) reduced parasite burden by 65%-67% [Ref1166:Bhowmick and Ali, 2009]. Ifng (Interferon gamma) Mouse 15978 33468859 NM_008337 NP_032363.1 MGI:107656; UniProt:P01580 10090 ? >gi|145966741|ref|NM_008337.3| Mus musculus interferon gamma (Ifng), mRNA ATAGCTGCCATCGGCTGACCTAGAGAAGACACATCAGCTGATCCTTTGGACCCTCTGACTTGAGACAGAA GTTCTGGGCTTCTCCTCCTGCGGCCTAGCTCTGAGACAATGAACGCTACACACTGCATCTTGGCTTTGCA GCTCTTCCTCATGGCTGTTTCTGGCTGTTACTGCCACGGCACAGTCATTGAAAGCCTAGAAAGTCTGAAT AACTATTTTAACTCAAGTGGCATAGATGTGGAAGAAAAGAGTCTCTTCTTGGATATCTGGAGGAACTGGC AAAAGGATGGTGACATGAAAATCCTGCAGAGCCAGATTATCTCTTTCTACCTCAGACTCTTTGAAGTCTT GAAAGACAATCAGGCCATCAGCAACAACATAAGCGTCATTGAATCACACCTGATTACTACCTTCTTCAGC AACAGCAAGGCGAAAAAGGATGCATTCATGAGTATTGCCAAGTTTGAGGTCAACAACCCACAGGTCCAGC GCCAAGCATTCAATGAGCTCATCCGAGTGGTCCACCAGCTGTTGCCGGAATCCAGCCTCAGGAAGCGGAA AAGGAGTCGCTGCTGATTCGGGGTGGGGAAGAGATTGTCCCAATAAGAATAATTCTGCCAGCACTATTTG AATTTTTAAATCTAAACCTATTTATTAATATTTAAAACTATTTATATGGAGAATCTATTTTAGATGCATC AACCAAAGAAGTATTTATAGTAACAACTTATATGTGATAAGAGTGAATTCCTATTAATATATGTGTTATT TATAATTTCTGTCTCCTCAACTATTTCTCTTTGACCAATTAATTATTCTTTCTGACTAATTAGCCAAGAC TGTGATTGCGGGGTTGTATCTGGGGGTGGGGGACAGCCAAGCGGCTGACTGAACTCAGATTGTAGCTTGT ACCTTTACTTCACTGACCAATAAGAAACATTCAGAGCTGCAGTGACCCCGGGAGGTGCTGCTGATGGGAG GAGATGTCTACACTCCGGGCCAGCGCTTTAACAGCAGGCCAGACAGCACTCGAATGTGTCAGGTAGTAAC AGGCTGTCCCTGAAAGAAAGCAGTGTCTCAAGAGACTTGACACCTGGTGCTTCCCTATACAGCTGAAAAC TGTGACTACACCCGAATGACAAATAACTCGCTCATTTATAGTTTATCACTGTCTAATTGCATATGAATAA AGTATACCTTTGCAACC >gi|33468859|ref|NP_032363.1| interferon gamma [Mus musculus] MNATHCILALQLFLMAVSGCYCHGTVIESLESLNNYFNSSGIDVEEKSLFLDIWRNWQKDGDMKILQSQI ISFYLRLFEVLKDNQAISNNISVIESHLITTFFSNSKAKKDAFMSIAKFEVNNPQVQRQAFNELIRVVHQ LLPESSLRKRKRSRC IFN-gamma plays a critical role in Th1 type immune response. It is important for protection against infections by various viruses and intracellular bacteria. Vaximmutor The experimental data demonstrated that three time vaccinations with BCG in BALB/c mice induced strong TB Ag-specific IFN-gamma immune responses in splenocytes [Ref2101:Wang et al., 2009]. Ighv1-9 Mus musculus 668478 AC073561 10090 12 114583568 114583861 immunoglobulin heavy variable V1-9 Also known as Igg2a; Gm16697 >gi|372099098:114583568-114583861 Mus musculus strain C57BL/6J chromosome 12, GRCm38 C57BL/6J GTCTTGCACAGTAATAGATGGCAGAGTCCTCAGTTGTCAGGCTGCTGAGTTGCATGTAGGCTGTGTTGGA GGATGTATCTGCAGTGAATGTGGCCTTGCCCTTGAACTTCTCATTGTAGTTAGTACTACCACTTCCAGGT AAAATCTCTCCAATCCACTCAAGGCCATGTCCAGGCCTCTGCTTTACCCACTCTATCCAGTAGCCAGTGA ATGTGTAGCCAGTAGCCTTGCAGGAAAGCTTCACTGAGGCCCCAGGCTTCATCAGCTCAGCTCCAGACTG CTGCAGCTGAACCT Vaximmutor Il2 Mus musculus 16183 7110653 DN-144H19.3 AF195954 NP_032392 10090 3 37120712 37125953 - interleukin 2 4.63 18506.61 169 Also known as Il-2 >gi|372099107:37120712-37125953 Mus musculus strain C57BL/6J chromosome 3, GRCm38 C57BL/6J ATTTTTTTTTAGAGGAGAGCTTTATTTCTTGAAAACACTGATTAACATAGAGTTCACAGGAATAACTGAG AAGTTATTTTAGCGCTTACTTTGTGCTGTCCTAAAAATGACAGACATCTGAGCTTATTTATATTTGAATC ATCTAAATACTTTTATTAATGAGTCTACCTACACATGATATTTAACAATTCAATATAATAAATAATTTCA GATAAATAGTTTAAAACATTTTTGAGCCCTTGGGGCTTACAAAAAGAATCTTTAAAGATCCATATTTATC ATCTGAAGACTAGTAGTTACAAAAGATAGTAAACAATACATCCAAAAATAAATTAAAGTTAAATATTTAA ATAAATAGAGAGCCTTATGTGTTGTAAGCAGGAGGTACATAGTTATTGAGGGCTTGTTGAGATGATGCTT TGACAGAAGGCTATCCATCTCCTCAGAAAGTCCACCACAGTTGCTGACTCATCATCGAATTGGCACTCAA ATGTGTTGTCAGAGCCCTAAAAAAGAATATAAAATTGTAGGCTAAGGTAGCTTACTTTGCATATAATTAT TCTTCACGGAAGCTTTTAGGCATTTATTTTAACACTGGTTAAATATATTGAACATTCACATTTCTGAAAT GATCACAATTATTGGGTTATGTTTTATTATGATATCAAATGGTAAAGCATAAAAAATAAAGCTCTCCAGA GTTGATTACCAACGAGCATTTGATGGGAACACTGAACACTTCTGTAGAATTCAGTTGCTTGACCACTTTT TCTCTGGTAAGTGTACACAGCTATGCATCAATTTAGGCTTCAGGAATGGAGAAATGATACTTGTTATATG TTCTTTGCTAAATCTTAAGAGTCTATTATTCAATTCTTTCCCCCCCAAGTCAGAATGGGAACAACCCAGA GTAGGTTAGGACAAGCATCTATTGGGGGAAATTTGGAGAATTTTGTTATAGATATACCTACCCTGATACC AGTGTAGATGAATCACAAAGTTTGTACATGTATAAATATTATAAATTTGTTCTGTGGATTAGCTTTTTGA AAGCTAACCCTCTTTGCTAAAGGAGATATTTTAATTCTGTTTTTAGGTGACAAGCTGAGAAGGAAATATT TTGACAAATTTATGGGATGGCTTTTCCAAATCTGACTAATTCCTTGTAAGTCAAATGAGGCAGATTATTC CTTTTAAATAAATACTCCTTTTCAAATAAGCTGCTGTGGTCTTATATACCCTCTTTACATAGCTACTTCA ATATTCTAATGTCTTGAATTTTTCATTTTTAAAAATATGTGGCCCTTGAAACATTTTTCTAGTTCTCATG TAGCTCTAAAGTTTGTACCATTCATTAGGGGTGAACTTTCTGATGTTGGCCATAGATTTTAGAGCATCCA TCTTTGCATACGTAAGTACTCGATTTTAGAGCATCCATCTTAGCATACGTAAGTACTCACACCTTTCAAC GTCTAGATGATGTGTATTTCAGCCTGCTTTAAAAACCTCAAATGGAAGCTGGGCAGTGGTGGTGCAGGCC TTTAATCCCAGCACTTGGGAGGCAGAGGCAGGCGGATTTCTGAGTTCGAGGCCAGCCTGGTCTACAGAGT GAGTTCCAGGACAGCCAGGGCTACACAGAGAAATCCTGTCTCAAAAAAACAAACAAACAAACAAACAAGA AACAAACAAACAAAAAAAACAAAAACAAACAAAACAAAACCTCAAATGGAAACAGTGCACTGAAATGTGA CTTTGGTTTGGAAAGGACTAGCCCACACCCTCTTGGAGGCTTGCTGCTACTGTCTCACCAGAGTCCATGA TTCTTGTGCATTTAAAAACAAAGCTCTGCAGTGGGCTCTCCCCGTCCTGCTCTGTCCATTTTAATGGCTG CCATTTTTGGAGAGAAATGTCTGTTTTTCTACCAATACCAGCACAACTTCTCTGGAAAAACTTTTCAGAT AATTTTTTCTGATCTGATGAATGTAACACCAGCAAGAGTTGCTTGTTTCTTGTGGAATTCTACTCCGTGC TTTCTCTCACATCCAGTTCTATGCTGGTGTGGAGGGAGCAGAGTGTTCATGTTCCCAGTTTCCTTGCAGG TGATGGTAGGTGGAAATTCTAGCATCATCCTACAGTGGAAGGATTCACTTGCACAGTGACTTTAAACTTT GGCTGACTAAATGCACAGAACCCATCAAAGACCAGAAATGGCAAGCCACTTAAAAATGCATTTCTTCTCT ATTTTATTTCCAGATTAGCAAATAAAGCAACACCTTACCTTTAGTTTTACAACAGTTACTCTGATATTGC TGATGAAATTCTCAGCATCTTCCAATTGAAAGCTTTTGCTTTGAGTCAAATCCAGAACATGCCGCAGAGG TCCAAGTTCATCTTCTAGGCACTGAAGATCTTTCAATTCTGTGGCCTAGAGGAGTAATAAGCTTAACCAT CAGCTCAGCTCACCACATACTGAAGAGCCAGAAAGTTAGTCTGCAGTCTCTCTAATCAAGAGAAGGCAGC ACATAGCTTTTACCACTCCCTGTCCTCTGTAAAGGGGGACTGAGGTAATCGATGCCATAAATCTAGAAGA GCAAGAGCTCACAACCATAAGGGTCACCTTGACTGTTAGGCCACTCTAGTGAGCTCTTCTGGCTTCATTA GACTTTGTAAAAAGTCTGTGTTTCTCTACCAATGCATAGCACAAGTTCAGACTATTGTTCCAATCTACAA AGAAATCTGCAAGGTTCACATTCTAATATCTAATCGCAGAGTTGAGAATCACAGAAGGGTAAGGGACAGG AATCCTTGGATGCCAACTGTCATAGGCCTAAATCTTACAGATTAGGTTATCATGGCCCTGACTGAGGGGT GTCAAGATAGCCAGGAAGACACATGTAATATTTTTTAAATTTATACTTCTCTGCAATTACTAAAGATGAG TTTTTTAAAAACCCATATGTCAAGCTAGGAAGATGGCTTTTAAGGTAAAGGTACCTGCCACCAAACTTGA TGATTTGAGTTCAATTGCAGTGACCCACCCACATTGTGGAAAGAATGGCCCAACTTTCATATTTCGTCTT CTGACCTCCACAGTTACACTGTGATACACATGCACCTCCACACATACATACATACATACATACATACATA CATACATACATACATACATACATACATAAAATGTAAAATCTATTTGTCCCAATGAAAAAAGTCATAACAT TTTGGCAGAACACTTGGGAGAATTTTTCTGATCCATGTATGAAATAATGTTTAAATACATCATGCATACT TACATACATATACAGGGAAAAAGGATATTGTCTAGCTCTATAGTACACTATGATTTCCATAAAGTCAGCT GCTTTAAGTCTACAGTGAACTGTGTTATCTCCATTTTACCAAGTCTCACAATCAGTGTCTTTCCCACAAC CACATGAACGGGGAGCAAGGGTGGCCCGGTCGGTCGGTCGCTCCTTTCATTAACCACAGCCTTTGAATTA CATGCTTCTATTGTTTTTAAAATCTTACATACCGAATGCAGGTTAAATGAAAACATCAGCAGAATTTACC ACATTACTCTTGTTTTCAATAATTATTTTAAAACTTAGATTTCTAGGAATTTCACCACTCTCTAAATTAA CATGATCTCTGTTGTTTCTCTAACAATCCTTAGAGGAAGAGGTTTGACAAGATAACACGTAGTTCCTGAT TGGTCTGCTATTGACCTTCCAACTTGTTATGGTGTGTCTTGGGTATTCAGTGTGGAGCTCCTTCCCTCAC AGAACTCTCCAGTTTGTTACTGTGGGAGCTGAACATTATGTGACTGTAATTAAGCTGGAAGAGCAACTGG GGCCTTTCTTTTTCATCTCCTGTAGAACAGCTAGAGGCAAAGTTCCCCTGACTCAATAGGAATGGGTCAA CAGCTGCCTCTTTGTCCCCTTAGATCCCATTTTGCTCTAGGCTTGGATTTACTTGGGACAAGCTCTTTCT AGGACCAAAGTTATCCATTCTCTTTTGACTTTCGGGACTAGAGCAAATTTCTACCCTTGCTGGAGTTCTA AGAGCTTGTGTAAGCTGTTTTGTATCACACAACATTCTGCCTCCAAAGGAGACCAAAAAACCTTTCAATA TTGAGAGATAGTATCATGTAGTAATATTACAGCTCTCTAGTTCCACTAGTTAAAAGAGACTGTATAAATC CAAAATTGTTTTATACATCTCGGACTTCTTCTCTAGCACTAATAGTGTGTTTATGTGCTGTTGGCCAGAC ACTGTTCTGAAACCTGACAAGTGATAAGCATAGCAATGATCATTTATGTAAGTGGGTGAATGAGCATAGA CAACTTCCTGAGGCCATGAGAGCTAGGCCCTAGCAGGGCTGGACTCCACTGCAGATCATTGGCCCTAGAA TCTTAACATTGGTTATGCTGCTCCTCAAAAATGCAGTCATAGGAATCATTCTTAAAACAGTAAAGTGTGT GTAAAATGAGACCCTCTCAAGTCAATTTTTACATTTAAGAAGCTGAAATAATGCACCTCTCTCAAATATC TGTAGGACAAGCATAAAACAGAAATCAACAGTCTTTAAATTATCCCAGCATCAAAATGCAATCATCTTGC ATTTTCTTCTCATTCCCTTTCCCAACACATAAATACACAGGAAAAATGTAAAGAAAACCATTTAAAAGAA GTACCATTGTCAAGATTTTTTTACAGAGAGATATCAGAGAAACTTATTTTCTTCAGATGAGGTACTATTC ATCTGGTCACATGTTATTTACACGTTATACACATGTATGTTACTTTGAATTCATTAGAGCACCAGTTAAA CACAGAAACTCACTCACCTGCTTGGGCAAGTAAAATTTGAAGGTGAGCATCCTGGGGAGTTTCAGGTTCC TGTAATTCTGAGAAAGCGTAACACATTATTATTAAAGGTTATTAAACACAGCCTTTGGCAAGAAAGCTAA AGGTATTGCCTATAGATGGGATGGCTGTGCACTTACCTCCATCCTGCTCAGGAGCTCCTGTAGGTCCATC AACAGCTGCTCCAGGTGCTGCTGCTGCTGCTGCTGCTGCTGCTGCTGCTGCTGTGCTTCCGCTGTAGAGC TTGAAGTGGAGCTTGAAGTGGGTGCGCTGTTGACAAGGAGCACAAGTGTCAATGTGACACAGGATGCGAG CTGCATGCTGTACATGCCTGCAGGACTTGAGGTCACTGTGAGGAGTGATTAGCAAGGGTGAT >gi|7110653|ref|NP_032392.1| interleukin-2 precursor [Mus musculus] MYSMQLASCVTLTLVLLVNSAPTSSSTSSSTAEAQQQQQQQQQQQQHLEQLLMDLQELLSRMENYRNLKL PRMLTFKFYLPKQATELKDLQCLEDELGPLRHVLDLTQSKSFQLEDAENFISNIRVTVVKLKGSDNTFEC QFDDESATVVDFLRRWIAFCQSIISTSPQ Vaximmutor KMP-11 Leishmania donovani VO_0011157 7579896 CDD:281087 5661 ? KMP-11 7.09 11872.82 150 Kinetoplastid membrane protein 11; pfam03037 >AAB33127.2 KMP-11 (kinetoplast) [Leishmania donovani] MATTYEEFSAKLDRLDQEFNRKMQEQNAKFFADKPDESTLSPEMREHYEKFERMIKEHTEKFNKKMHEHS EHFKQKFAELLEQQKAAQYPSK Protective antigen KMP-11 DNA vaccination alone in an experimental BALB/c mice model showed significant potential in terms of resolution of splenic and hepatic parasite burden against virulent LD challenge. KMP-11 DNA immunization significantly protects against L. donovani infection [Ref1167:Bhaumik et al., 2009]. mspC Leishmania donovani VO_0011158 21954466 CDD:302875 GOA:Q8MM48 HSSP:1LML InterPro:IPR001577 UniProtKB/TrEMBL:Q8MM48 5661 ? GP63 6.49 63738.41 691 Leishmanolysin; cl19482 >CAD42816.1 GP63 [Leishmania donovani] MSVDSSSTHRHRSVAARLVRLAAAGAAVIAAVGTAAAWAHAGAVQHRCIHDAMHPRVRQSVARHHTAPGA VSAVGLPYVTLDTAAAADRRPGSAPTVVRAANWGALRIAVSTEDLTDPAYHCARVGQRVNNHAGAIATCT ADDILTDEKRDILVKYLIPQALQLHTERLKVRQVQDKWKVTDMVDEICGDFKVPPAHITDGLSNTDFVMY VASVPSEEGVLAWATTCQVFSDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHALGFSGTFFTEILVV TQMMNIRGKDFNVSVINSSTAVAKAREQYGCGTLEYLEIEDQGGAGSAGSHIKMRNAKDELMAPAAAAGY YSALTMAIFQDLGFYQADFSKAEEMPWGRNAGCAFLSEKCMEQNITKWPAMFCNVSVDVVRCPTSRLMLG TCGIRGYSTPFSPYWQYFTNISLGGYSPFLDYCPFVIGYGDGSCNQDASLATGFFGAFNVFSDAARCIDG AFRPKNRTAADGYYAGLCANVRCDTATRTYSVQVCGSMDYVNCTPGLRVELSTVSSAFEEGGYITCPPYV EVCQANVKGAKDFAGDSDSSSSAGDAADRAAMQRWNDRMAGLATAAMVLLGMVLSLMALVVVWLLLLTCP WWCCKFGGLPT Protective antigen Study showed that cationic distearoyl phosphatidylcholine (DSPC) liposomes, when used as vaccine adjuvant with the immunodominant 63-kDa glycoprotein (gp63, mspC) of Leishmania donovani promastigotes, induced significant protection against progressive visceral leishmaniasis in susceptible BALB/c mice. gp63 used without adjuvant elicited partial protection but in association with liposomes exhibited marked resistance in both the livers and spleens of the mice challenged 10 days after the last vaccination [Ref1168:Bhowmick et al., 2008]. NH Leishmania donovani VO_0011161 19697561 CDD:239117 5661 ? nucleoside hydrolase 6.51 30583.64 375 nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, xanthosine-inosine-uridine-adenosine-preferring and, uridine-cytidine preferring nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the...; cd02651 >AAG02281.1 nucleoside hydrolase [Leishmania donovani] MPRKIILDCDPGIDDAVAIFLAHGNPEVELLAITTVVGNQTLEKVTRNARLVADVAGIVGVPVAAGCTKP LVRGVRNASQIHGETGMGNVSYPPEFKTKLDGRHAVQLIIDLIMSHEPKTITLVPTGGLTNIAMAVRLEP RIVDRVKEVVLMGGGYHTGNASPVAEFNVFVDPEAAHIVFNESWNVTMVGLDLTHQALATPAVQKRVKEV GTKPAAFMLQILDFYTKVYEKERNTYATVHDPCAVAYVIDPTVMTTEQVPVDIELNGALTTGMTVADFRY PRPKHCHTQVAVKLDFDKFWCLVIDALKRIGDPQ Protective antigen Experimental infection of immunized BALB/c mice demonstrated that the VR1012-NH36 DNA vaccine derived from the nucleoside hydrolase gene (NH) of L. donovani induced an 88% reduction in L. chagasi parasite load and a 65% reduction in L. mexicana lesion size [Ref1171:Aguilar-Be et al., 2005]. ORFF Leishmania donovani VO_0011159 703122 5661 ? unknown 5.32 29594.74 334 >AAA96728.1 unknown [Leishmania donovani] MQSDARELNPGRADFWEHFYGQEDGRLQQKELHHRKAREIVERGSLMNHYEWFMQYPMYEAALKACLRAV PTVLSKDGATRILHTGCGNSDFCDHVEGLLSDLNPAPSSSSRTCEVLNVDICENIVTHLALHFPSRLYAV GDCCDLHVSSSPSMPFSSNAAWYSRDTALRLRTVLQSSVDVVFDKGTADALLSSFAGVCNPNMEAYVGEA LKVLRPGGLLFLISINSEDVLSPYVLSAGDGLKSFQLAYADVIELCAQDLRHLRVETLGSRYSCYGYAVV ASAVAE Protective antigen An expression plasmid encoding both p35 and p40 subunits of IL-12 when co-administered with a recombinant open-reading frame (rORFF) gene from the LD1 locus of Leishmania donovani induces significant protection with around 82% protection in both liver and spleen of BALB/c mice when challenged with L. donovani [Ref1169:Tewary et al., 2006]. P1 27465165 27465166 AAN60108.1 CDD:100109 5661 ? ribosomal protein P1-like protein 4.09 11317.016 182 Ribosomal protein P1. This subfamily represents the eukaryotic large ribosomal protein P1. Eukaryotic P1 and P2 are functionally equivalent to the bacterial protein L7/L12, but are not homologous to L7/L12. P1 is located in the L12 stalk, with proteins...; cd05831 >gi|27465165|gb|AY161269.1| Leishmania donovani ribosomal protein P1-like protein mRNA, complete cds AATTCGTGTACTTTATTAGCACGTCATCACAGAGAACACCTTCCTTACGCACTGTCCATCATCGCCATGT CCGCTGAGACCCTCGCGTGCACGTACGCCGCGCTCATGCTGAGTGACGCCGGCCTGCCCACCTCGGCCGA GAACATCGCCGCGGCGGTGAAGGCGGCCGGCGTCGAGATGCGCCCCACCCTGCCCATCATCTTTGCCCGC TTCCTGGAGAAGAAGTCCGTGGAGACGCTGATGGCGGCCGCCGCCGCGCAGGCCCCGACGGCCGCGTNCG CCCCGTCTCCGGCGGCGGGCGCCGCCTCCGCTGCANCGGNCGGCGGCAAGGTGGAGGACAAGAAGAAGGA CGAGCCTGAGGAAGAGGGCGACGACGACATGGGTTTTGGTCTGTTCGACTGAGCGCCCCGCATGATGACC GGCATATGCGAGCACATGGTTGTTTGGCCTCATGTTCTGCAACACCCGAGCATGCCGTGAGCGCTGCCTC TCTGCGTGCACATATATATATATGTGTGTGTGTGTGTGTGCGTGTGTTTCGCTGCTCTCTTTTTCTTTTC GATTTTATTTACGTGTGCGTTACTCCTTCCTCCTGCGAAAAAAAAAAAAAAAAAAAA >AAN60108.1 ribosomal protein P1-like protein [Leishmania donovani] MSAETLACTYAALMLSDAGLPTSAENIAAAVKAAGVEMRPTLPIIFARFLEKKSVETLMAAAAAQAPTAA XAPSPAAGAASAAXXGGKVEDKKKDEPEEEGDDDMGFGLFD Protective antigen DNA vaccine pVAX-P1 in a prime-boost mode was able to induce protection with reduced mortality, a significant (75.68%) decrease in splenic parasite burden and increased expression of Th1 type cytokines in immunized hamsters [Ref2053:Arora et al., 2011]. TNF-alpha Mus musculus 21926 7305585 AB039224 NP_038721 10090 17 35199389 35201995 - tumor necrosis factor 4.75 24010.47 235 Also known as DIF; Tnfa; TNFSF2; Tnfsf1a; TNFalpha; TNF-alpha; MGC151434 >gi|372099093:35199389-35201995 Mus musculus strain C57BL/6J chromosome 17, GRCm38 C57BL/6J CTTTATTTCTCTCAATGACCCGTAGGGCGATTACAGTCACGGCTCCCGTGGGGAGCAGAGGTTCAGTGAT GTAGCGACAGCCTGGTCACCAAATCAGCGTTATTAAGACAATTGGGTTAGATAAATATTTTGTTTTAAAC ATAAGCAAAAGAGGAGGCAACAAGGTAGAGAGGCCAGGTGGGGACAGCTCAGCTCCGTTTTCACAGAAAA CATGTCTGTCTGAAGACAGCTTCCCACACTGGGTCCTCCAGGACACCCCGGCCTTCCAAATAAATACATT CATAAGCAAATAAATAAATAATAAATAAATAATAAATAATAAGTGCAAATATAAATAGAGGGGGGCTGGC TCTGTGAGGAAGGCTGTGCATTGCACCTCAGGGAAGAATCTGGAAAGGTCTGAAGGTAGGAAGGCCTGAG ATCTTATCCAGCCTCATTCTGAGACAGAGGCAACCTGACCACTCTCCCTTTGCAGAACTCAGGAATGGAC ATTCGAGGCTCCAGTGAATTCGGAAAGCCCATTTGAGTCCTTGATGGTGGTGCATGAGAGGCCCACAGTC CAGGTCACTGTCCCAGCATCTTGTGTTTCTGAGTAGTTGTTGAAAGCTCTGAGCACAGAGTTGGACCCTG AGCCATAATCCCCTTTCTAAGTTAGAAGGATACAGACTGGGGGCTCTGAGGAGTAGACAATAAAGGGGTC AGAGTAAAGGGGTCAGAGTGGGGGCTGGGTAGAGAATGGATGAACACCCATTCCCTTCACAGAGCAATGA CTCCAAAGTAGACCTGCCCGGACTCCGCAAAGTCTAAGTACTTGGGCAGATTGACCTCAGCGCTGAGTTG GTCCCCCTTCTCCAGCTGGAAGACTCCTCCCAGGTATATGGGCTCATACCAGGGTTTGAGCTCAGCCCCC TCAGGGGTGTCCTTGGGGCAGGGGCTCTTGACGGCAGAGAGGAGGTTGACTTTCTCCTGGTATGAGATAG CAAATCGGCTGACGGTGTGGGTGAGGAGCACGTAGTCGGGGCAGCCTTGTCCCTTGAAGAGAACCTGGGA GTAGACAAGGTACAACCCATCGGCTGGCACCACTAGTTGGTTGTCTTTGAGATCCATGCCGTTGGCCAGG AGGGCGTTGGCGCGCTGGCTCAGCCACTCCAGCTGCTCCTCCACTTGGTGGTTTGCTGAGGGGGGGGGGG AGGATTGAGTCAGTGTCACCCTCTTAGTTCACACTCCACATCCTGAGCCTCAGCAGCTACCCACACTTCA CTTCCGGTTCCTGCACCCTCTGTCTTTCCACATCCCATTGGCTATGAGGTCCCGGGTGGCCCCCTGATGC CTTGCTTTTGAGTCACTGCTCTGACTCTCACGTGCTGTCTCTAAGAGCTCTGTCTTTTCTCAGCCTGGCT CGACACCCCTCAACCCGCCCCCCAAAATCATGCCCCTTCATTCTCAAGGCACATGTAAAGAAATCTTACC TACGACGTGGGCTACAGGCTTGTCACTCGAATTTTGAGAAGATGATCCTGGAGGGGAAGAGACAAAGGCA AGGATGAGCCTTTTAGGCTTCCCAGCAAGCATCTATGCACTTAGACCCCTTTCCTCCCAAACCAAAGCTT TAAGTTCTCCCCCCACCCCATCTCATCCCATGCCTAACTGCCCTTCCTCCATCTTAAATTAAGAGAGAGG TGTGGGAACACTTACTGAGTGTGAGGGTCTGGGCCATAGAACTGATGAGAGGGAGGCCATTTGGGAACTT CTGTGTAGGAAAAGGAGGTTAGTTAAGACAGACTCACCCCAAAGGAGAAGCCTCCCGGCTGATTGCCCCG CTTACAGTTCCTCTTTGCCCCACCCCACCCCCCAGCTTTGTGTTTTTCTTCTTCATTCATTCATCTGTCC AACCCACGGCTTCTTTCTGCGGTGCCCTCTGTGCTTGATCTCCCGTTATCTCCCCTTCATCTTCCTCCTT ATCTCTCATGCCTCTCTCATTTCTGTCTCTGAGTTTTATCTCTTGCTTATCCCCTCTTCCCCTGGCCACA TCTTTCCAGATCTCTCCACGTGTGAACACACTTGTTCGTTCATTCATCTCTCTGTGCATCCGACGAAGGA TGTTTAGTCAGCTGGACGCATGGGTCCGAGGTCCTGACTCTGTCCCCTCCACACTCTCCTCCACCTTGCC CTGCCCATTAGCCCACTTCTTTCCCTCACACTGTCCTTCTTGCCCTCCTAACCCGTTTTGCTTGTGAGCG AGAATAAGGGTTGCCCAGACACTCACCTCATCCCTTTGGGGACCGATCACCCCGAAGTTCAGTAGACAGA AGAGCGTGGTGGCCCCTGCCACAAGCAGGAATGAGAAGAGGCTGAGACATAGGCACCGCCTGGAGTTCTG GAAGCCCCCCATCTTTTGGGGGAGTGCCTCTTCTGCCAGTTCCACGTCGCGGATCATGCTTTCTGTGCTC ATGGTGTCTTTTCTGGAGGGAGATGTGGCGCCTTGGGCCAGTGAGTGAAAGGGACAGAACCTGCCTGGTT GGCTGCTTGCTTTTCTGGGAGCTATTTCCAAGATGTTCTGGAGTTTCTGTTCTCCCTCCTGGCTAGTCCC TTGCTGTCCTCGCTGAG >gi|7305585|ref|NP_038721.1| tumor necrosis factor [Mus 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