title: Inhibition of binding of hamster antibody to myelin basic protein by a synthetic triproline-containing peptide from JC virus T-antigen.
abstract: Antisera raised against porcine myelin basic protein (MBP) in Syrian hamsters were assayed by an ELISA method. The specificity of a high-titered antiserum was probed with synthetic peptides representing a hexapeptide and a decapeptide of the JC virus (JCV) large T-antigen C-terminus which is homologous to the MBP triproline region, a decapeptide from MBP which is encephalitogenic in guinea pigs, and peptides unrelated to MBP, i.e., substance P and poly-L-lysine. In an ELISA inhibition assay, preincubation of the hamster antiserum to MBP with either the JCV T-antigen C-terminal decapeptide or the encephalitogenic determinant inhibited binding activity in a dose-dependent manner. In contrast, the T-antigen C-terminal hexapeptide, substance P, and poly-L-lysine were not inhibitory. These results suggest that the triproline region of MBP can be immunogenic in hamsters, and support the concept that a conformation of the MBP triproline region is shared with certain of its viral homologues. In an effort to detect similar cross-reactive specificities in hamster antisera to JCV T-antigen, sera of 50 hamsters bearing subcutaneous tumors induced by JCV-transformed glial cells were tested for ability to bind to MBP in the ELISA assay. While significant increases in response compared to prebleed levels were observed in about one-fourth of the sera, some of them showed similar increases in binding to other basic proteins such as histones, and the binding to MBP was not inhibited by the triproline-containing decapeptide.
mesh_terms: D000818:Animals; D000906:Antibodies / Q000276:immunology*; D000918:Antibody Specificity; D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor / Q000276:immunology*; D001667:Binding, Competitive; D006224:Cricetinae; D003429:Cross Reactions; D007577:JC Virus / Q000276:immunology; D004676:Myelin Basic Protein / Q000276:immunology* / Q000378:metabolism; D009856:Oncogene Proteins, Viral / Q000276:immunology*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000276:immunology; D011392:Proline / Q000276:immunology / Q000378:metabolism; D013552:Swine
chemical_list: D000906:Antibodies; D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor; D004676:Myelin Basic Protein; D009856:Oncogene Proteins, Viral; D010446:Peptide Fragments; D011392:Proline