title: Integrin alphavbeta1 is a receptor for foot-and-mouth disease virus.
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 alphavbeta3 and the epithelial integrin alphavbeta6. In this report we show that the integrin alphavbeta1, when expressed as a human/hamster heterodimer on transfected CHOB2 cells, is a receptor for FMDV. Virus binding and infection mediated by alphavbeta1 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 alpha5/alphav integrin subunits, in association with the beta1 chain, to bind FMDV and mediate infection matched the ligand binding specificity of alphavbeta1, not alpha5beta1, thus providing further evidence for the receptor role of alphavbeta1. In addition, data are presented suggesting that amino acid residues near the RGD motif may be important for differentiating between the binding specificities of alphavbeta1 and alphavbeta6.
authors.affiliation: Department of Molecular Biology, Institute for Animal Health, Pirbright, Surrey GU24 ONF, UK. terry.jackson@bbsrc.ac.uk
authors.forename: Terry
authors.initials: T
authors.lastname: Jackson
authors.forename: A Paul
authors.initials: AP
authors.lastname: Mould
authors.forename: Dean
authors.initials: D
authors.lastname: Sheppard
authors.forename: Andrew M Q
authors.initials: AM
authors.lastname: King
mesh_terms: D000818:Animals; D015703:Antigens, CD / Q000235:genetics / Q000378:metabolism; D000951:Antigens, Neoplasm; D016466:CHO Cells; D002118:Calcium / Q000378:metabolism; D002213:Capsid / Q000378:metabolism; D036022:Capsid Proteins; D002413:Cations, Divalent; D002460:Cell Line; D006224:Cricetinae; D029544:Foot-and-Mouth Disease Virus / Q000378:metabolism*; D006801:Humans; D039564:Integrin alphaV; D019012:Integrin beta1 / Q000235:genetics / Q000378:metabolism; D016023:Integrins / Q000235:genetics / Q000378:metabolism*; D008274:Magnesium / Q000378:metabolism; D008345:Manganese / Q000378:metabolism; D009842:Oligopeptides / Q000378:metabolism*; D017469:Receptors, Fibronectin / Q000235:genetics / Q000378:metabolism; D011991:Receptors, Virus / Q000235:genetics / Q000378:metabolism*; D019030:Receptors, Vitronectin
chemical_list: D015703:Antigens, CD; D000951:Antigens, Neoplasm; D036022:Capsid Proteins; D002413:Cations, Divalent; D039564:Integrin alphaV; D019012:Integrin beta1; D016023:Integrins; D009842:Oligopeptides; D017469:Receptors, Fibronectin; D011991:Receptors, Virus; D019030:Receptors, Vitronectin; C442501:VP1 protein, Foot-and-mouth disease virus; C064660:integrin alphaVbeta5; C094340:integrin alphavbeta1; C073878:integrin alphavbeta6; D008345:Manganese; C047981:arginyl-glycyl-aspartic acid; D008274:Magnesium; D002118:Calcium