Recently, this laboratory has developed a comprehensive strategy for the systematic localization of all the 'continuous' antigenic (as well as other binding) sites of complex multivalent protein antigens involved in B and T cell recognition. The strategy depends on the synthesis of consecutive overlapping peptides that together account for the entire protein chain. 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 protein chain of lysozyme were synthesized and examined for their ability to stimulate in vitro proliferation of T cells from several mouse strains (A/J, H-2a; BALB/c and DBA/2, H-2d; B10.BR, H-2k; DBA/1, H-2q; SJL, H-2s) that had been primed with native 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, three of which were subject to individual control.
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