Proteolytic Processing of Human Cytomegalovirus Glycoprotein B Is Dispensable for Viral Growth in Culture

Open Access
Publisher Website
Google Scholar
Abstract
Infection by field strains of Foot-and-mouth disease virus (FMDV) is initiated by binding to certain species of arginine-glycine-aspartic acid (RGD)-dependent integrin including αvβ3 and the epithelial integrin αvβ6. In this report we show that the integrin αvβ1, when expressed as a human/hamster heterodimer on transfected CHOB2 cells, is a receptor for FMDV. Virus binding and infection mediated by αvβ1 was inefficient in the presence of physiological concentrations of calcium and magnesium but were significantly enhanced by reagents that activate the integrin and promote ligand binding. The ability of chimeric α5/αv integrin subunits, in association with the β1 chain, to bind FMDV and mediate infection matched the ligand binding specificity of αvβ1, not α5β1, thus providing further evidence for the receptor role of αvβ1. In addition, data are presented suggesting that amino acid residues near the RGD motif may be important for differentiating between the binding specificities of αvβ1 and αvβ6.