title: Protein chimeras containing the Mycoplasma bovis GAPDH protein and bovine host-defence peptides retain the properties of the individual components.
abstract: Besides the well characterized role in glycolysis, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been implicated in virulence of pathogenic micro-organisms and because of its cell surface location, it has been shown to act as an adhesin for colonization of tissue surfaces both for pathogenic and non-pathogenic normal microflora. These novel properties of GAPDH make this protein a target for studies in pathogenesis and a candidate for vaccine development against several diseases. Previously, we have isolated the GAPDH protein of Mycoplasma bovis and we are currently using this protein as a test antigen to develop a vaccine to protect feedlot animals from M. bovis-related diseases. As part of our vaccine studies, we are testing several novel immune modulators, some of which are host-defence peptides (HDP). HDP are small protein molecules that are part of the innate immune system of the host possess antimicrobial activities and can act as adjuvants. These novel compounds have been used as part of chimeric proteins composed of viral antigens fused to HDP and these chimeras were found to promote immune responses. The first step in the use of the M. bovis GAPDH protein and HDP as components of a vaccine was to construct M. bovis GAPDH-HDP chimeric proteins. The three M. bovis GAPDH-HDP chimeric proteins constructed here: GAPDH-BMAP28 (sGap-M), GAPDH-indolicidin (sGap-I), and GAPDH-TAP (Gap-T) retained properties associated with the individual components, namely GAPDH enzymatic and HDP antimicrobial activities.
authors.affiliation: Vaccine and Infectious Disease Organization (VIDO), University of Saskatchewan, 120 Veterinary Rd, Saskatoon, SK, Canada S7N 5E3.
authors.forename: Jacques
authors.initials: J
authors.lastname: van der Merwe
authors.forename: Tracy
authors.initials: T
authors.lastname: Prysliak
authors.forename: Volker
authors.initials: V
authors.lastname: Gerdts
authors.forename: Jose
authors.initials: J
authors.lastname: Perez-Casal
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000096:biosynthesis / Q000737:chemistry / Q000494:pharmacology; D000956:Antigens, Viral / Q000096:biosynthesis; D001428:Bacterial Vaccines / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D002417:Cattle; D023082:Defensins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*; D015964:Gene Expression Regulation, Bacterial; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*; D007113:Immunity, Innate; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D045682:Mycoplasma bovis / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*
chemical_list: D000900:Anti-Bacterial Agents; D000956:Antigens, Viral; D001428:Bacterial Vaccines; D023082:Defensins; D011993:Recombinant Fusion Proteins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases