Analysis of the Heterogeneity of the Binding Site Specificities of Hyperimmune Human Anti‐A and ‐A,B Sera: The Application of Competition Assays Using Murine Monoclonal Antibodies

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Abstract
Monoclonal antibodies PL41 and AL62 have previously been shown to recognize two distinct blood group A epitopes on the red cell surface. Competitive inhibition of the binding of 125I-PL41 and 125I-AL62 to group A1 red cells, by hyperimmune polyclonal human antibodies, has been employed to investigate the binding site specificities of 15 anti-A and 8 anti-A,B sera. Differences in the degree of inhibition of the binding of the two MABs by individual anti-A or -A,B samples indicate that polyclonal reagents are composed to varying proportions of up to 3 (or more) different antibody specificities, each recognizing distinct epitope: PL41-like, AL62-like and a third (as yet undefined) category of antibody. In general, those anti-A sera with PL41-like specificities are superior agglutinators of A2B cells with weakly expressed A antigens; similarly, the specificity of potent anti-A,B sera capable of strongly agglutinating Ax cells was likewise directed towards PL41-binding blood group A trisaccharide haptens.

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