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The SDR1 monoclonal antibody reacts only with cells which express the HLA-DR1, 2,w6 or w8 allogeneic specificities. Two-dimensional nonequilibrium pH gradient/sodium dodecyl sulfate polyacrylamide gel electrophoretic analyses of SDR1 immunoprecipitates from [35S]methionine biosynthetically labeled cells revealed the typical pattern of Ia antigens, namely two polypeptides of about 34kDa and 29kDa (designated epsilon and beta-3) as well as the "basic invariant spot" of about 31 kDa. The epsilon and beta-3 polypeptides were only weakly represented in similar analyses of immunoprecipitates performed using a monomorphic HLA-DR monoclonal antibody, TDR31.1. The epsilon and beta-3 polypeptides of B lymphoblastoid cell lines homozygous for HLA-DR2 and w6 were structurally polymorphic as judged by two-dimensional gel analyses. This polymorphism was independent of the HLA-DR specificity. It is concluded that the SDR1 antibody recognizes a polymorphic set of Ia antigens that are coded by a locus other than HLA-DR. These antigens probably also express the MT1 (DC1, LB12) alloantigenic specificity and are most likely the human equivalent of the murine I-A subregion antigens.

Original publication

DOI

10.1002/eji.1830120713

Type

Journal article

Journal

Eur J Immunol

Publication Date

07/1982

Volume

12

Pages

600 - 606

Keywords

Animals, Antibodies, Monoclonal, Antibody Specificity, B-Lymphocytes, Binding Sites, Antibody, Cell Line, Chemical Precipitation, Chromosome Mapping, Electrophoresis, Polyacrylamide Gel, Genes, MHC Class II, Glycoproteins, HLA-DR Antigens, Histocompatibility Antigens Class II, Humans, Lectins, Mice, Peptides, Rabbits