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Science 22 November 1991:
Vol. 254. no. 5035, pp. 1200 - 1202
DOI: 10.1126/science.1957171
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Articles
Science, Vol 254, Issue 5035, 1200-1202
Copyright © 1991 by American Association for the Advancement of Science
Structurally homologous ligand binding of integrin Mac-1 and viral glycoprotein C receptors
DC Altieri,
OR Etingin,
DS Fair,
TK Brunck,
JE Geltosky,
DP Hajjar,
and
TS Edgington
Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.
Three spatially distant surface loops were found to mediate the interaction of the coagulation protein factor X with the leukocyte integrin Mac-1. This interacting region, which by computational modeling defines a three-dimensional macromotif in the catalytic domain, was also recognized by glycoprotein C (gC), a factor X receptor expressed on herpes simplex virus (HSV)-infected endothelial cells. Peptidyl mimicry of each loop inhibited factor X binding to Mac-1 and gC, blocked monocyte generation of thrombin, and prevented monocyte adhesion to HSV-infected endothelium. These data link the ligand recognition of Mac-1 to established mechanisms of receptor-mediated vascular injury.
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