Molecular Identification of a Surface Structure on B Cells (Lyb-3) and Its Relationship to B Cell Triggering

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Abstract
Lactoperoxidase-catalyzed radioiodination of cell surface proteins and immunochemical procedures are used to identify murine splenic lymphocyte membrane components bound by anti-Lyb-3 serum. This antiserum defines membrane components (Lyb-3) on a subpopulation of murine B cells that may function as a receptor for T cell signals. SDS-PAGE analysis of surface-labeled membrane components bound by anti-Lyb-3 serum demonstrated a single molecular species of 68,000 d. The polypeptides recognized by anti-Lyb-3 are not composed of disulfide-linked subunits and bear no antigenic relationship with known membrane immunoglobulins (IgM or IgD). Absorption of anti-Lyb-3 serum with the 68,000 d polypeptides removed the ability of anti-Lyb-3 serum to augment the in vivo immune response of mice to low doses of sheep erythrocytes. The latter provides formal proof that the 68,000 d polypeptide bound by anti-Lyb-3 serum is the target on the B cell membrane for the immunoenhancing activity of the antiserum.