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 α and β 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 TRa1, a B-lymphoblastoid cell line (B-LCL). Two-dimensional electrophoresis and Western blotting of TRa1 glycoproteins showed that these species had the appropriate electrophoretic mobilities for class I heavy chain and class II α and β subunits. The presence of the epitope was verified on class II α and β subunits by Western blotting of purified αβ-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 (β 2m) was difficult to detect by Western blotting, binding of PAC.M1 to purified β 2m was detectable in a solid-phase binding assay. Thus, PAC.Ml reacts with a determinant shared by a number of members of the immunoglobulin superfamily.
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Lutz, P.M., Cresswell, P. An epitope common to HLA class I and class II antigens, Ig light chains, and β 2-microglobulin. Immunogenetics 25, 228–233 (1987). https://doi.org/10.1007/BF00404692
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DOI: https://doi.org/10.1007/BF00404692