HUMAN ‘Ia’ ANTIGEN POPULATIONS DEFINED BY MONOCLONAL ANTIBODIES

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Abstract
The relationships between the antigens recognized by 4 monoclonal anti-human Ia-like antibodies were investigated using sequential immunoprecipitation and capping techniques. Two of the antibodies were monomorphic and were previously shown to recognize epitopes in which carbohydrate residues are involved, whereas the two polymorphic antibodies recognized protein-defined epitopes.sbd.one of these epitopes being present on MB+DR- molecules. In the absence of an indisputable anti-DR monoclonal antibody, it was not possible to conclusively verify which Ia-encoded antigens were detected by the anti-Ia-like monoclonal antibodies. Several firm conclusions could be drawn: so-called monomorphic antibodies do not necessarily react with all Ia molecules encoded by a single locus.sbd.from the results using the 2 monomorphic antibodies, B5.1 and 3F1.1, described herein, 2 populations of antigens being B5.1+3F1.1+ and B5.1+3F1.1- were identified; cross-reactivity of a polymorphic determinant expressed on antigenically-separable Ia molecules was noted.sbd.using the 2 polymorphic antibodies, 26.1 and F5C9, molecules which were 26.1+F5C9+ and 26.1-F5C9+ were identified; and the data clearly point to the existence of at least 2 loci coding for Ia-like antigens (one of which may or may not be the HLA-DR locus). Given that polymorphisms can now include protein- and carbohydrate-defined epitopes, that cross-reactions occur and that the definition of DR itself by monoclonal antibodies is not clear, the complexity of the human Ia antigens is apparent.