Abstract
The leucocyte surface glycoproteins CD11a (gp160, LFA-1 antigen, TA-1 antigen), CD11b (gp155, Mac-1 antigen, OKM1 antigen, Mo-1 antigen), CD11c (gp130, Leu-M5 antigen), and CD18 (gp90) constitute three heterodimers with different alpha chains and a common beta chain. Monoclonal antibodies to CD11a, b, or c block adhesion of certain types of leucocytes only, while several antibodies to CD18 inhibit adhesion in all of them. The functionally important site or sites on CD18 are not known. We have now isolated the CD11a,b,c-CD18 leucocyte antigen complex in large amounts from human leucocytes, and produced several new monoclonal antibodies reacting with CD18. One of these antibodies, like those described earlier, inhibits leucocyte adhesion, whereas the others do not. By means of competition experiments, at least four epitope regions were found. These antibodies should be valuable in elucidating the regions essential in CD18-mediated leucocyte functions.
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