PMID: 6400996Jan 1, 1984Paper

T-cell recognition of lysozyme. I. Localization of regions stimulating T-cell proliferative response by synthetic overlapping peptides encompassing the entire molecule

Experimental and Clinical Immunogenetics
G S BixlerM Z Atassi

Abstract

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.

Related Concepts

Related Feeds

Bacterial Cell Wall Structure (ASM)

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.

Bacterial Cell Wall Structure

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.