T-cell recognition of lysozyme. I. Localization of regions stimulating T-cell proliferative response by synthetic overlapping peptides encompassing the entire molecule.
The systematic localization of the full antigenic profile for T-cell recognition of a complex multivalent protein antigen has not been accomplished. Recently, this laboratory has developed a comprehensive strategy for the localization of all the continuous antigenic (as well as other binding) sites of a protein. The strategy depends on the synthesis of consecutive overlapping peptides that together systematically account for the entire polypeptide chain of the protein. This strategy was applied here for the localization of the 'continuous' T-cell recognition sites of hen egg lysozyme. Eight overlapping peptides encompassing the entire primary structure of lysozyme were synthesized and examined for their ability to stimulate in vitro proliferation of T cells from two high responder mouse strains (H-2k and H-2q) that had been primed with lysozyme. This approach enabled the identification of a full profile of in vitro active lysozyme peptides and the localization of four major T-cell recognition sites.
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D007114:Immunization; D008198:Lymph Nodes / Q000276:immunology; D008213:Lymphocyte Activation; D051379:Mice; D008810:Mice, Inbred C57BL / Q000276:immunology; D008811:Mice, Inbred DBA / Q000276:immunology; D008969:Molecular Sequence Data; D009113:Muramidase / Q000235:genetics / Q000276:immunology*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000276:immunology; D013601:T-Lymphocytes / Q000276:immunology*
D010446:Peptide Fragments; D009113:Muramidase