Abstract
THE antigen receptors on mature B lymphocytes are membrane-bound immunoglobulins of the IgM and IgD classes1,2 whose cross-linking by polyvalent antigens results in B-cell proliferation and differentiation3. How these membrane-bound immunoglobulin chains, which lack a cytoplasmic tail, generate a cell activation signal is not at present known. We now show that the IgM molecule is non-covalently associated in the membrane of B cells with two proteins of relative molecular mass 34,000 (Mr 34 K; IgM-α) and 39 K (Ig-β) which form a disulphide-linked heterodimer. Surface expression of IgM seems to require the formation of an appropriate complex between IgM and the heterodimer. A transfection experiment indicates that IgM-α is the product of mb-l, a B-cell-specific gene4encoding a transmembrane protein with sequence homology5 to proteins of the T-cell antigen receptor–CD3 complex6–8.
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Hombach, J., Tsubata, T., Leclercq, L. et al. Molecular components of the B-cell antigen receptor complex of the IgM class. Nature 343, 760–762 (1990). https://doi.org/10.1038/343760a0
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DOI: https://doi.org/10.1038/343760a0
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