An epitope common to HLA class I and class II antigens, Ig light chains, and beta 2-microglobulin

Abstract

The homology of class I major histocompatibility complex (MHC) antigens, class II MHC antigens, and immunoglobulin molecules has suggested their divergence from a common ancestral gene. We report here a monoclonal antibody (mAb), PAC.M1, which reacts with HLA class I heavy chains, HLA class II alpha and beta chains, and the light chain of human immunoglobulin by Western blot analysis. PAC.M1 reacted with 44 kd, 33 kd, and 29 kd species when tested on membrane glycoproteins from TRal, a B-lymphoblastoid cell line (B-LCL). Two-dimensional electrophoresis and Western blotting of TRal glycoproteins showed that these species had the appropriate electrophoretic mobilities for class I heavy chain and class II alpha and beta subunits. The presence of the epitope was verified on class II alpha and beta subunits by Western blotting of purified alpha beta-invariant chain complexes, and on class I heavy chains by Western blotting of purified class I antigens. The PAC.M1 mAb also reacted with immunoglobulin light chains when Western blotting was performed with normal human serum and purified IgG and IgM as antigens. While reactivity of the mAb with beta-2 microglobulin (beta 2m) was difficult to detect by Western blotting, binding of PAC.M1 to purified beta 2m was detectable in a solid-phase binding assay. Thus, PAC.M1 reacts with a determinant shared by a number of members of the immunoglobulin superfamily.