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Journal of Virology, September 2004, p. 9773-9781, Vol. 78, No. 18
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.18.9773-9781.2004

Interactions of Foot-and-Mouth Disease Virus with Soluble Bovine {alpha}Vß3 and {alpha}Vß6 Integrins

Hernando Duque,{dagger}, Michael LaRocco, William T. Golde, and Barry Baxt*

Foot-and-Mouth Disease Research Unit, Plum Island Animal Disease Center, USDA Agricultural Research Service, Greenport, New York

Received 8 January 2004/ Accepted 16 May 2004

At least four members of the integrin family of receptors, {alpha}Vß1, {alpha}Vß3, {alpha}Vß6, and {alpha}Vß8, have been identified as receptors for foot-and-mouth disease virus (FMDV) in vitro. Our investigators have recently shown that the efficiency of receptor usage appears to be related to the viral serotype and may be influenced by structural differences on the viral surface (H. Duque and B. Baxt, J. Virol. 77:2500-2511, 2003). To further examine these differences, we generated soluble {alpha}Vß3 and {alpha}Vß6 integrins. cDNA plasmids encoding the individual complete integrin {alpha}V, ß3, and ß6 subunits were used to amplify sequences encoding the subunits' signal peptide and ectodomain, resulting in subunits lacking transmembrane and cytoplasmic domains. COS-1 cells were transfected with plasmids encoding the soluble {alpha}V subunit and either the soluble ß3 or ß6 subunit and labeled with [35S]methionine-cysteine. Complete subunit heterodimeric integrins were secreted into the medium, as determined by radioimmunoprecipitation with specific monoclonal and polyclonal antibodies. For the examination of the integrins' biological activities, stable cell lines producing the soluble integrins were generated in HEK 293A cells. In the presence of divalent cations, soluble {alpha}Vß6 bound to representatives of type A or O viruses, immobilized on plastic dishes, and significantly inhibited viral replication, as determined by plaque reduction assays. In contrast, soluble {alpha}Vß3 was unable to bind to immobilized virus of either serotype; however, virus bound to the immobilized integrin, suggesting that FMDV binding to {alpha}Vß3 is a low-affinity interaction. In addition, soluble {alpha}Vß3 did not neutralize virus infectivity. Incubation of soluble {alpha}Vß6 with labeled type A12 or O1 resulted in a significant inhibition of virus adsorption to BHK cells, while soluble {alpha}Vß3 caused a low (20 to 30%), but consistent, inhibition of virus adsorption. Virus incubated with soluble {alpha}Vß6 had a lower sedimentation rate than native virus on sucrose density gradients, but the particles retained all of their structural proteins and still contained bound integrin and, therefore, were not exhibiting characteristics of a picornavirus A particle.

* Corresponding author. Mailing address: USDA, ARS, Plum Island Animal Disease Center, P.O. Box 848, Greenport, NY 11944-0848. Phone: (631) 323-3354. Fax: (631) 323-3006. E-mail: bbaxt{at}piadc.ars.usda.gov.

{dagger} Present address: USDA Animal Plant Health Inspection Service, Veterinary Services, Foreign Animal Disease Diagnostic Laboratory, Greenport, NY 11944.

Journal of Virology, September 2004, p. 9773-9781, Vol. 78, No. 18
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.18.9773-9781.2004




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