The immune response to Epstein-Barr nuclear antigen: conformational and structural features of antibody binding to synthetic peptides.
Naturally developing human antibodies to the Epstein-Barr nuclear antigen recognize synthetic peptides containing sequences from the unusual glycine-alanine region of this protein. We tested antibody binding to a series of peptides of from five to 20 amino acids in length. Peptides as small as seven amino acids could bind but optimal results required chain lengths of 15. Binding was extremely sensitive to small changes in the length and sequence of the peptide, and also to the temp of the reaction. The changes can be ascribed to two factors: (1) deletion of the site of antigen binding and (2) loss of peptide secondary structure.
D000595:Amino Acid Sequence; D000818:Animals; D000917:Antibody Formation; D000941:Antigens / Q000276:immunology; D000956:Antigens, Viral / Q000276:immunology*; D001666:Binding Sites, Antibody; D001667:Binding, Competitive; D002467:Cell Nucleus / Q000276:immunology; D002942:Circular Dichroism; D004797:Enzyme-Linked Immunosorbent Assay; D019309:Epstein-Barr Virus Nuclear Antigens; D004854:Herpesvirus 4, Human / Q000276:immunology*; D006801:Humans; D010455:Peptides / Q000276:immunology*; D011487:Protein Conformation; D011817:Rabbits; D013696:Temperature
D000941:Antigens; D000956:Antigens, Viral; D019309:Epstein-Barr Virus Nuclear Antigens; D010455:Peptides