Abstract
Results with two well-characterized self-antigens, cytochrome c and myelin basic protein, have led to differing opinions regarding the predominant specificities of autoantibodies, whether regions of sequence diversity or 'structurally inherent features' of a protein determine favored antigenic sites. To further examine this question, 16 antibody epitopes have been mapped on a highly immunopathogenic autoantigen, retinal S-antigen (S-Ag). The epitopes were characterized for: (1) sequence diversity and cross-reactivity on S-antigens from several species; (2) conformational dependency; and (3) probability of their occurrence on the surface of S-antigen. A single C-terminal region containing sequence diversity was most frequently recognized, but no evidence for recognition of any other regions of sequence diversity was found. Thirteen of 16 monoclonal antibodies raised to native S-Ag bound epitopes strongly predicted to be on the surface of S-antigen. Conversely, only one of six antibody preparations raised to peptides or affinity-purified on peptides was found to recognize an epitope predicted to be on the surface, suggesting a good correlation between specificity for conformation-dependent sites and surface probability based on t...Continue Reading
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