Immune recognition of human major histocompatibility antigens: localization by a comprehensive synthetic strategy of the continuous antigenic sites in the first domain of HLA‐DR2 β chain

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Abstract
A comprehensive synthetic approach, previously developed in this laboratory, has been applied to screen the entire first domain (residues 1–95) of the HLA-DR2 β chain for the full profile of continuous regions that are recognized by human alloantisera and anti-DR or anti-β chain antisera raised in other species. Nine consecutive peptides, that were 15 residues each and overlapped by 5 residues, covering the first domain of the DR2 β chain were synthesized, purified and characterized. The antibody-binding activities of the peptides were determined by radioimmunosorbent titrations. This established the full profile of peptides having specific antibody-binding activity with these various antisera. Three continuous antigenic sites were localized in this domain by all of antisera tested. Peptide 81–95 appeared to be the most immunodominant (i.e. bound the highest amounts of antibodies) in most antisera tested. Although their immunodominance varied with the antisera and boundary shifts were present, the submolecular regions recognized on the first domain of DR2β appeard to be similar with antisera against the DR2 (αβ1) complex or against the isolated β chain. Furthermore, recognition was independent of the host species from which the antisera were obtained.

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