Induction and characterization of antisera against terminal and internal peptides of SV40 large T antigen.
Thirteen synthetic peptides corresponding to different regions of the SV40 large T antigen were used as immunogens after coupling to a carrier protein. All peptide conjugates elicited sera that recognized the inducing peptide. In 10 cases the corresponding sites in the native large T antigen also were recognized, as determined by immunoprecipitation. The degree of recognition of the native protein varied between 0.5 and 80%, the most reactive sera being those induced by the terminal peptides. The ability of internal peptides to induce antibodies reactive with native large T antigen appeared to be correlated with peptide hydrophilicity and possibly atomic mobility. No such correlation was apparent with predicted features of secondary structure. The influence of peptide length on induction of protein-recognizing antisera will also be discussed.
D000595:Amino Acid Sequence; D000818:Animals; D000918:Antibody Specificity; D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor / Q000032:analysis* / Q000276:immunology / Q000502:physiology; D002352:Carrier Proteins; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology; D007106:Immune Sera / Q000302:isolation & purification*; D007114:Immunization / Q000379:methods; D009856:Oncogene Proteins, Viral / Q000032:analysis* / Q000276:immunology / Q000502:physiology; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism; D011233:Precipitin Tests / Q000379:methods; D011817:Rabbits / Q000276:immunology; D013329:Structure-Activity Relationship
D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor; D002352:Carrier Proteins; D000939:Epitopes; D007106:Immune Sera; D009856:Oncogene Proteins, Viral; D010455:Peptides