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Journal of Virology, February 2002, p. 935-941, Vol. 76, No. 3
0022-538X/01/$04.00+0     DOI: 10.1128/JVI.76.3.935-941.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Integrin vß1 Is a Receptor for Foot-and-Mouth Disease Virus

Department of Molecular Biology, Institute for Animal Health, Pirbright, Surrey GU24 ONF,¹ Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom,² Lung Biology Center, Cardiovascular Research Institute, Department of Medicine, University of California, San Francisco, California 94143-0854³

Received 30 July 2001/ Accepted 30 October 2001

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 vß3 and the epithelial integrin vß6. In this report we show that the integrin vß1, when expressed as a human/hamster heterodimer on transfected CHOB2 cells, is a receptor for FMDV. Virus binding and infection mediated by vß1 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 5/v integrin subunits, in association with the ß1 chain, to bind FMDV and mediate infection matched the ligand binding specificity of vß1, not 5ß1, thus providing further evidence for the receptor role of vß1. In addition, data are presented suggesting that amino acid residues near the RGD motif may be important for differentiating between the binding specificities of vß1 and vß6.

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