D. T. Fearon authored a 1980 study identifying a membrane glycoprotein as the receptor for the complement fragment C3b on human red blood cells, B cells, monocytes and polymorphonuclear leukocytes. The molecule, called gp205 in the paper, is associated with the receptor now called complement receptor 1. The work connected a purified protein's biochemical activity with a receptor found on several classes of blood cells.[ref]
Identification of the membrane glycoprotein that is the C3b receptor of the human erythrocyte, polymorphonuclear leukocyte, B lymphocyte, and monocyte by D. T. Fearon. Abstract, Journal of Experimental Medicine 152 (1980), pp. 20–30; DOI 10.1084/jem.152.1.20.
The route to identification is instructive. The glycoprotein was investigated for its ability to inhibit a C3 convertase and to assist enzymatic inactivation of C3b. Those activities suggested a C3b-binding function, which the receptor experiments tested. Thus a cell membrane receptor need not merely initiate a response: recognition of a complement component can also help regulate the amplification system to which that component belongs.[ref]
Identification of the membrane glycoprotein that is the C3b receptor of the human erythrocyte, polymorphonuclear leukocyte, B lymphocyte, and monocyte by D. T. Fearon. Abstract: convertase destabilization, C3b-inactivator cofactor activity and receptor identification.
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