{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T13:12:04Z","timestamp":1793020324594,"version":"4.5.0"},"reference-count":68,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2016,2,1]],"date-time":"2016-02-01T00:00:00Z","timestamp":1454284800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100000038","name":"National Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Canadian Bacterial Diseases Network"},{"DOI":"10.13039\/100010710","name":"Dairy Farmers of Canada","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100010710","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100015754","name":"Dairy Farmers of Ontario","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100015754","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Alberta Milk Producers","id":[{"id":"https:\/\/ror.org\/04f6sph74","id-type":"ROR","asserted-by":"crossref"}]},{"name":"British Columbia Innovation Agriculture Fund"},{"DOI":"10.13039\/100008921","name":"Saskatchewan Agriculture Development Fund","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100008921","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Canadian Bovine Mastitis Research Network (Now Canadian Bovine Mastitis and Milk Quality Research Network)"},{"name":"The Alberta Agriculture Research Institute"},{"DOI":"10.13039\/501100005019","name":"Beef Cattle Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005019","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Alberta Livestock Industry Development Fund"},{"name":"Agriculture and Food Council of Alberta, Ontario Cattlemen's Association","id":[{"id":"https:\/\/ror.org\/02zsyc904","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Advancing Agriculture and Agri-Food (ACAAF) Program"},{"DOI":"10.13039\/501100002715","name":"Alberta Livestock and Meat Association","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002715","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["clinicalkey.jp","clinicalkey.com","clinicalkey.es","clinicalkey.com.au","clinicalkey.fr","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Vaccine"],"published-print":{"date-parts":[[2016,2]]},"DOI":"10.1016\/j.vaccine.2015.11.072","type":"journal-article","created":{"date-parts":[[2015,12,15]],"date-time":"2015-12-15T23:13:26Z","timestamp":1450221206000},"page":"1012-1017","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":54,"title":["Glyceradehyde-3-phosphate dehydrogenase as a suitable vaccine candidate for protection against bacterial and parasitic diseases"],"prefix":"10.1016","volume":"34","author":[{"given":"Jose","family":"Perez-Casal","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew A.","family":"Potter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.vaccine.2015.11.072_bib0345","doi-asserted-by":"crossref","first-page":"2271","DOI":"10.1016\/0024-3205(96)00123-3","article-title":"Minireview. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells","volume":"58","author":"Sirover","year":"1996","journal-title":"Life Sci"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0350","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/S0167-4838(99)00119-3","article-title":"New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase","volume":"1432","author":"Sirover","year":"1999","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0355","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1016\/j.bbagen.2011.05.010","article-title":"On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control","volume":"1810","author":"Sirover","year":"2011","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0360","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1016\/S0021-9258(19)75833-5","article-title":"Identification of the 37-kDa protein displaying a variable interaction with the erythroid cell membrane as glyceraldehyde-3-phosphate dehydrogenase","volume":"262","author":"Allen","year":"1987","journal-title":"J Biol Chem"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0365","doi-asserted-by":"crossref","first-page":"2065","DOI":"10.1084\/jem.170.6.2065","article-title":"The major parasite surface antigen associated with human resistance to schistosomiasis is a 37-kD glyceraldehyde-3P-dehydrogenase","volume":"170","author":"Goudot-Crozel","year":"1989","journal-title":"J Exp Med"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0370","doi-asserted-by":"crossref","first-page":"2597","DOI":"10.1128\/IAI.57.9.2597-2605.1989","article-title":"Mapping of the human plasmin domain recognized by the unique plasmin receptor of group A streptococci","volume":"57","author":"Broder","year":"1989","journal-title":"Infect Immun"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0375","doi-asserted-by":"crossref","first-page":"5204","DOI":"10.1128\/jb.174.16.5204-5210.1992","article-title":"Cloning, sequence analysis, and expression in Escherichia coli of a streptococcal plasmin receptor","volume":"174","author":"Lottenberg","year":"1992","journal-title":"J Bacteriol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0380","doi-asserted-by":"crossref","first-page":"2311","DOI":"10.1099\/13500872-142-8-2311","article-title":"The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase","volume":"142","author":"Winram","year":"1996","journal-title":"Microbiology"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0385","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1006\/bbrc.2000.3884","article-title":"Analysis of expression of a cytosolic enzyme on the surface of Streptococcus pyogenes","volume":"278","author":"D\u2019Costa","year":"2000","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0390","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1099\/00221287-144-8-2025","article-title":"Site-directed mutagenesis of streptococcal plasmin receptor protein (Plr) identifies the C-terminal Lys334 as essential for plasmin binding, but mutation of the plr gene does not reduce plasmin binding to group A streptococci","volume":"144","author":"Winram","year":"1998","journal-title":"Microbiology"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0395","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1016\/S0923-2508(97)88080-1","article-title":"Group A streptococcal isolate 64\/14 expresses surface plasmin-binding structures in addition to Plr","volume":"148","author":"D\u2019Costa","year":"1997","journal-title":"Res Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0400","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1084\/jem.176.2.415","article-title":"A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity","volume":"176","author":"Pancholi","year":"1992","journal-title":"J Exp Med"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0405","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.jmb.2005.04.063","article-title":"Group A streptococcal surface GAPDH, SDH, recognizes uPAR\/CD87 as its receptor on the human pharyngeal cell and mediates bacterial adherence to host cells","volume":"350","author":"Jin","year":"2005","journal-title":"J Mol Biol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0410","doi-asserted-by":"crossref","first-page":"3544","DOI":"10.1128\/IAI.64.9.3544-3547.1996","article-title":"Monoclonal antibodies that recognize a common pneumococcal protein with similarities to streptococcal group A surface glyceraldehyde-3- phosphate dehydrogenase","volume":"64","author":"Kolberg","year":"1996","journal-title":"Infect Immun"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0415","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1128\/IAI.72.4.2416-2419.2004","article-title":"Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein","volume":"72","author":"Bergmann","year":"2004","journal-title":"Infect Immun"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0420","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1128\/IAI.70.3.1254-1259.2002","article-title":"Identification of major outer surface proteins of Streptococcus agalactiae","volume":"70","author":"Hughes","year":"2002","journal-title":"Infect Immun"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0425","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1139\/w03-042","article-title":"Characterization of group B streptococcal glyceraldehyde-3-phosphate dehydrogenase: surface localization, enzymatic activity, and protein-protein interactions","volume":"49","author":"Seifert","year":"2003","journal-title":"Can J Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0430","doi-asserted-by":"crossref","first-page":"5475","DOI":"10.1128\/IAI.72.9.5475-5477.2004","article-title":"Characterization of binding of Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase to Porphyromonas gingivalis major fimbriae","volume":"72","author":"Maeda","year":"2004","journal-title":"Infect Immun"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0435","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1111\/j.1432-1033.1996.0042u.x","volume":"239","author":"Gase","year":"1996","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0440","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/j.vetmic.2004.05.008","article-title":"Cloning and purification of the Streptococcus suis serotype 2 glyceraldehyde-3-phosphate dehydrogenase and its involvement as an adhesin","volume":"102","author":"Brassard","year":"2004","journal-title":"Vet Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0445","doi-asserted-by":"crossref","first-page":"1819","DOI":"10.1016\/S0140-6736(02)08713-5","article-title":"Genome and virulence determinants of high virulence community-acquired MRSA","volume":"359","author":"Baba","year":"2002","journal-title":"Lancet"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0450","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.vetmic.2003.12.009","article-title":"Characterization of two proteins of Staphylococcus aureus isolated from clinical mastitis with homology to glyceraldehyde-3-phosphate dehydrogenase","volume":"99","author":"Goji","year":"2004","journal-title":"Vet Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0455","doi-asserted-by":"crossref","first-page":"1225","DOI":"10.1016\/S0140-6736(00)04403-2","article-title":"Whole genome sequencing of meticillin-resistant Staphylococcus aureus","volume":"357","author":"Kuroda","year":"2001","journal-title":"Lancet"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0460","doi-asserted-by":"crossref","first-page":"1603","DOI":"10.1046\/j.1365-2958.2002.02850.x","article-title":"Transferrin binding in Staphylococcus aureus: involvement of a cell wall-anchored protein","volume":"43","author":"Taylor","year":"2002","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0465","doi-asserted-by":"crossref","first-page":"2278","DOI":"10.1016\/S0264-410X(02)00114-7","article-title":"Immunisation of dairy cattle with recombinant Streptococcus uberis GapC or a chimeric CAMP antigen confers protection against heterologous bacterial challenge","volume":"20","author":"Fontaine","year":"2002","journal-title":"Vaccine"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0470","doi-asserted-by":"crossref","first-page":"1086","DOI":"10.1128\/IAI.67.3.1086-1092.1999","article-title":"The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase","volume":"67","author":"Modun","year":"1999","journal-title":"Infect Immun"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0475","doi-asserted-by":"crossref","first-page":"1956","DOI":"10.1128\/IAI.64.6.1956-1960.1996","article-title":"Iron starvation causes release from the group A streptococcus of the ADP-ribosylating protein called plasmin receptor or surface glyceraldheyde-3-phosphate-dehydrogenase","volume":"64","author":"Eichenbaum","year":"1996","journal-title":"Infect Immun"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0480","doi-asserted-by":"crossref","first-page":"6355","DOI":"10.1128\/AEM.00455-06","article-title":"Proteomic profiling and identification of immunodominant spore antigens of Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis","volume":"72","author":"Delvecchio","year":"2006","journal-title":"Appl Environ Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0485","doi-asserted-by":"crossref","first-page":"3646","DOI":"10.1128\/IAI.73.6.3646-3658.2005","article-title":"Comparative secretome analyses of three Bacillus anthracis strains with variant plasmid contents","volume":"73","author":"Lamonica","year":"2005","journal-title":"Infect Immun"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0490","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1186\/1477-5956-5-11","article-title":"Bacillus anthracis secretome time course under host-simulated conditions and identification of immunogenic proteins","volume":"5","author":"Walz","year":"2007","journal-title":"Proteome Sci"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0495","doi-asserted-by":"crossref","first-page":"2111","DOI":"10.1016\/j.bbapap.2010.08.004","article-title":"Surface localized and extracellular glyceraldehyde-3-phosphate dehydrogenase of Bacillus anthracis is a plasminogen-binding protein","volume":"1804","author":"Matta","year":"2010","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0500","doi-asserted-by":"crossref","first-page":"1112","DOI":"10.1099\/mic.0.2006\/000901-0","article-title":"Extracellular proteins of Lactobacillus crispatus enhance activation of human plasminogen","volume":"153","author":"Hurmalainen","year":"2007","journal-title":"Microbiology"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0505","doi-asserted-by":"crossref","first-page":"1667","DOI":"10.1111\/j.1365-2672.2007.03679.x","article-title":"Cell surface Lactobacillus plantarum LA 318 glyceraldehyde-3-phosphate dehydrogenase (GAPDH) adheres to human colonic mucin","volume":"104","author":"Kinoshita","year":"2008","journal-title":"J Appl Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0510","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/j.resmic.2008.07.005","article-title":"Cell surface glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Lactobacillus plantarum LA 318 recognizes human A and B blood group antigens","volume":"159","author":"Kinoshita","year":"2008","journal-title":"Res Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0515","doi-asserted-by":"crossref","first-page":"1190","DOI":"10.1016\/j.biocel.2007.03.008","article-title":"Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: interaction of the extracellular enzyme with human plasminogen and fibrinogen","volume":"39","author":"Egea","year":"2007","journal-title":"Int J Biochem Cell Biol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0520","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1016\/j.biocel.2012.03.002","article-title":"Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli","volume":"44","author":"Aguilera","year":"2012","journal-title":"Int J Biochem Cell Biol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0525","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1186\/1471-2180-10-280","article-title":"The role of glyceraldehyde 3-phosphate dehydrogenase (GapA-1) in Neisseria meningitidis adherence to human cells","volume":"10","author":"Tunio","year":"2010","journal-title":"BMC Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0530","series-title":"Identification of a plasmin receptor on Pasteurella haemolytica","author":"Potter","year":"1990"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0535","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/j.ijmm.2014.12.021","article-title":"Excretion of cytosolic proteins (ECP) in bacteria","volume":"305","author":"Gotz","year":"2015","journal-title":"Int J Med Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0540","doi-asserted-by":"crossref","first-page":"1635","DOI":"10.4014\/jmb.0902.0102","article-title":"Lactobacillus plantarum 299v surface-bound GAPDH: a new insight into enzyme cell walls location","volume":"19","author":"Saad","year":"2009","journal-title":"J Microbiol Biotechnol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0545","doi-asserted-by":"crossref","first-page":"e0125377","DOI":"10.1371\/journal.pone.0125377","article-title":"Streptococcus pneumoniae GAPDH is released by cell lysis and interacts with peptidoglycan","volume":"10","author":"Terrasse","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0550","first-page":"187","article-title":"NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase","volume":"12","author":"Aguilera","year":"2009","journal-title":"Int Microbiol: Off J Span Soc Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0555","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/j.exppara.2007.04.016","article-title":"Entamoeba histolytica: ADP-ribosylation of secreted glyceraldehyde-3-phosphate dehydrogenase","volume":"117","author":"Alvarez","year":"2007","journal-title":"Exp Parasitol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0560","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.molbiopara.2014.02.005","article-title":"Extracellular functions of glycolytic enzymes of parasites: unpredicted use of ancient proteins","volume":"193","author":"Gomez-Arreaza","year":"2014","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0565","doi-asserted-by":"crossref","first-page":"2039","DOI":"10.1016\/S0264-410X(99)00521-6","article-title":"Identification of a candidate vaccine peptide on the 37kDa Schistosoma mansoni GAPDH","volume":"18","author":"Argiro","year":"2000","journal-title":"Vaccine"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0570","doi-asserted-by":"crossref","first-page":"2033","DOI":"10.1016\/S0264-410X(99)00523-X","article-title":"Induction of a protection against S. mansoni with a MAP containing epitopes of Sm37-GAPDH and Sm10-DLC. Effect of coadsorbtion with GM-CSF on alum","volume":"18","author":"Argiro","year":"2000","journal-title":"Vaccine"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0575","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1016\/S0020-7519(01)00244-2","article-title":"Immunisation with Salmonella typhimurium-delivered glyceraldehyde-3-phosphate dehydrogenase protects mice against challenge infection with Echinococcus multilocularis eggs","volume":"31","author":"Muller-Schollenberger","year":"2001","journal-title":"Intl J Parasitol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0580","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.bbadis.2004.12.010","article-title":"Cloning, characterization and DNA immunization of an Onchocerca volvulus glyceraldehyde-3-phosphate dehydrogenase (Ov-GAPDH)","volume":"1741","author":"Erttmann","year":"2005","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0585","doi-asserted-by":"crossref","first-page":"5861","DOI":"10.1016\/j.vaccine.2015.07.110","article-title":"DNA vaccine encoding the moonlighting protein Onchocerca volvulus glyceraldehyde-3-phosphate dehydrogenase (Ov-GAPDH) leads to partial protection in a mouse model of human filariasis","volume":"33","author":"Steisslinger","year":"2015","journal-title":"Vaccine"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0590","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1139\/w04-016","article-title":"Use of the surface proteins GapC and Mig of Streptococcus dysgalactiae as potential protective antigens against bovine mastitis","volume":"50","author":"Bolton","year":"2004","journal-title":"Can J Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0595","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1111\/j.1365-2249.2004.02628.x","article-title":"Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse","volume":"138","author":"Ling","year":"2004","journal-title":"Clin Exp Immunol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0600","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1099\/0022-1317-51-8-661","volume":"51","author":"Rosinha","year":"2002","journal-title":"J Med Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0605","doi-asserted-by":"crossref","first-page":"814","DOI":"10.1006\/jmbi.1996.0204","article-title":"Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity","volume":"257","author":"Duee","year":"1996","journal-title":"J Mol Biol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0610","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1016\/j.pep.2003.09.011","article-title":"A GapC chimera retains the properties of the Streptococcus uberis wild-type GapC protein","volume":"33","author":"Perez-Casal","year":"2004","journal-title":"Protein Expr Purif"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0615","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.vetimm.2006.04.004","article-title":"DNA-protein immunization against the GapB and GapC proteins of a mastitis isolate of Staphylococcus aureus","volume":"113","author":"Kerro-Dego","year":"2006","journal-title":"Vet Immunol Immunopathol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0620","doi-asserted-by":"crossref","first-page":"1417","DOI":"10.1046\/j.1365-2958.2003.03518.x","article-title":"Surface localized glyceraldehyde-3-phosphate dehydrogenase of Mycoplasma genitalium binds mucin","volume":"48","author":"Alvarez","year":"2003","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0625","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/j.micinf.2007.01.004","article-title":"MSG1, a surface-localised protein of Mycoplasma suis is involved in the adhesion to erythrocytes","volume":"9","author":"Hoelzle","year":"2007","journal-title":"Microbes Infect"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0630","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.vetimm.2009.04.016","article-title":"Analysis of the immunoproteome of Mycoplasma mycoides subsp. mycoides small colony type reveals immunogenic homologues to other known virulence traits in related Mycoplasma species","volume":"131","author":"Jores","year":"2009","journal-title":"Vet Immunol Immunopathol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0635","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.micpath.2007.05.009","article-title":"Detection of antibodies against the Mycoplasma bovis glyceraldehyde-3-phosphate dehydrogenase protein in beef cattle","volume":"43","author":"Perez-Casal","year":"2007","journal-title":"Microb Pathog"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0640","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.micpath.2010.11.008","article-title":"Protein chimeras containing the Mycoplasma bovis GAPDH protein and bovine host-defence peptides retain the properties of the individual components","volume":"50","author":"van der Merwe","year":"2011","journal-title":"Microb Pathog"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0645","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.micpath.2012.12.001","article-title":"Vaccination with recombinant Mycoplasma bovis GAPDH results in a strong humoral immune response but does not protect feedlot cattle from an experimental challenge with M. bovis","volume":"55","author":"Prysliak","year":"2013","journal-title":"Microb Pathog"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0650","doi-asserted-by":"crossref","first-page":"5376","DOI":"10.1016\/j.vaccine.2009.06.072","article-title":"Vaccination with the M. suis recombinant adhesion protein MSG1 elicits a strong immune response but fails to induce protection in pigs","volume":"27","author":"Hoelzle","year":"2009","journal-title":"Vaccine"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0655","doi-asserted-by":"crossref","first-page":"1587","DOI":"10.1111\/j.1365-2672.2007.03386.x","article-title":"Characterization of OmpK, GAPDH and their fusion OmpK-GAPDH derived from Vibrio harveyi outer membrane proteins: their immunoprotective ability against vibriosis in large yellow croaker (Pseudosciaena crocea)","volume":"103","author":"Zhang","year":"2007","journal-title":"J Appl Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0660","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1111\/j.1348-0421.2005.tb03652.x","article-title":"Vaccine efficacy of recombinant GAPDH of Edwardsiella tarda against Edwardsiellosis","volume":"49","author":"Liu","year":"2005","journal-title":"Microbiol Immunol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0665","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.vetimm.2012.09.036","article-title":"Immune response of turbot (Scophthalmus maximus L.) to a broad spectrum vaccine candidate, recombinant glyceraldehyde-3-phosphate dehydrogenase of Edwardsiella tarda","volume":"150","author":"Liang","year":"2012","journal-title":"Vet Immunol Immunopathol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0670","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1472-765X.2011.03164.x","article-title":"Secreted glyceraldehyde-3-phosphate dehydrogenase as a broad spectrum vaccine candidate against microbial infection in aquaculture","volume":"54","author":"Li","year":"2012","journal-title":"Lett Appl Microbiol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0675","doi-asserted-by":"crossref","first-page":"982","DOI":"10.4014\/jmb.0901.007","article-title":"Evaluation of optimal culture conditions for recombinant ghost bacteria vaccine production with the antigen of Streptococcus iniae GAPDH","volume":"19","author":"Ra","year":"2009","journal-title":"J Microbiol Biotechnol"},{"key":"10.1016\/j.vaccine.2015.11.072_bib0680","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.1016\/j.vaccine.2008.12.047","article-title":"Identification and characterization of a novel protective antigen, Enolase of Streptococcus suis serotype 2","volume":"27","author":"Zhang","year":"2009","journal-title":"Vaccine"}],"container-title":["Vaccine"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0264410X15017661?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0264410X15017661?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,5,29]],"date-time":"2022-05-29T07:49:23Z","timestamp":1653810563000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0264410X15017661"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,2]]},"references-count":68,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2016,2]]}},"alternative-id":["S0264410X15017661"],"URL":"https:\/\/doi.org\/10.1016\/j.vaccine.2015.11.072","relation":{},"ISSN":["0264-410X"],"issn-type":[{"value":"0264-410X","type":"print"}],"subject":[],"published":{"date-parts":[[2016,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Glyceradehyde-3-phosphate dehydrogenase as a suitable vaccine candidate for protection against bacterial and parasitic diseases","name":"articletitle","label":"Article Title"},{"value":"Vaccine","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.vaccine.2015.11.072","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}