The continuous antigenic regions in the second domain of the β chain of human MHC DR2 antigen: antigenic profile of the entire extracellular part of the chain

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Abstract
Ten consecutive 15-residue peptides (except for peptide 181–198) that spanned the entire second domain of the HLA DR2 β chain and overlapped by 5 residues were synthesized, purified and characterized. The antibody-binding activities of the peptides with human alloantisera and with antisera raised in other species were determined by radioimmunosorbent titrations. This established the full profile of peptides having specific antibody-binding activity with these various antisera. The continuous antigenic sites in this domain were localized within four regions. The localization of the antigenic regions on the second domain completes the description of the antigenic profile of the entire extracellular part of the β chain of HLA DR2. Thus, the continuous antigenic sites on the extracellular part of the DR2 β subunit reside within seven regions with an eighth site being recognized somewhat weakly with some antisera. As was found for the first domain, the immunodominance of a given site varied with the antisera and boundary shifts were present. The submolecular regions recognized on the second domain of the DR2 β were independent of the host species from which the antisera were obtained.

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