Epitope mapping and conformational analysis of SV40 T-antigen deletion mutants.
Deletion mutants of SV40 T-antigen were stably expressed in BALB/c 3T3E cells and characterized in immunoprecipitation assays using T-antigen-specific monoclonal antibodies. The epitope recognized by antibody PAb602 was narrowed to T-antigen residues 230-362. Coprecipitation results were compatible with a p53-binding region between T-antigen amino acids 347 and 517. Amino terminal deletions (1-108 or 98-229) of T-antigen appeared to have pronounced effects on the conformation of distal regions of the molecule, based both on antibody binding and on association with p53.
Sawai
E T
ET
Division of Molecular Virology, Baylor College of Medicine, Houston, Texas 77030.
Butel
J S
JS
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000952:Antigens, Polyomavirus Transforming / Q000235:genetics / Q000276:immunology* / Q000648:ultrastructure; D002460:Cell Line; D004252:DNA Mutational Analysis; D000939:Epitopes; D051379:Mice; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000235:genetics / Q000276:immunology; D013329:Structure-Activity Relationship
D000911:Antibodies, Monoclonal; D000952:Antigens, Polyomavirus Transforming; D000939:Epitopes; D011994:Recombinant Proteins