pl50/95, Third member of the LFA‐1/CR3 polypeptide family identified by anti‐Leu M5 monoclonal antibody

Monoclonal antibody (mAb) anti‐Leu M5 reacts with a two‐chain molecule composed of a 150‐kDa α subunit noncovalently associated with a 95‐kDa β subunit and probably is specific for an epitope on the 150‐kDa β chain. This pl50/95 antigen is the third member of a family of polypeptides sharing a common 95‐kDa β chain, which includes the lymphocyte function‐associated antigen LFA‐1 (p177/95) and complement receptor CR3 (Mo1/MAC‐1/OKM1; p165/95) antigens. Sequential immunoprecipitation with anti‐p95 β chain mAb specifically removed the antigens detected by anti‐LFA‐1, anti‐CR3 and anti‐Leu M5 mAb. Certain patients with recurrent bacterial infections are genetically deficient in expression of the LFA‐1 and Mo1 antigens, and have impaired granulocyte function. Granulocytes from a patient with this disease also failed to react with anti‐Leu M5. Stimulation of normal granulocytes with f‐Met‐Leu‐Phe, C5a‐desArg, or calcium ionophore resulted in increased expression of Mo1 and Leu M5 antigens on the cell surface, but did not significantly increase expression of LFA‐1 antigen. In functional assays, anti‐Leu M5 did not inhibit T cell‐mediated or natural killer cell‐mediated cytotoxicity. In addition, anti‐Leu M5 neither inhibited the binding of complement‐coated particles to CR1 or CR3 nor did it affect the binding of EC3dg to neutrophils (CR4). These studies clearly indicate that the p150/95 antigen recognized by the anti‐Leu M5 antibody is a structurally distinct member of the LFA‐ 1/CR3 family.

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