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Journal of Virology, February 2003, p. 2500-2511, Vol. 77, No. 4
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.4.2500-2511.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Foot-and-Mouth Disease Virus Receptors: Comparison of Bovine {alpha}V Integrin Utilization by Type A and O Viruses

Hernando Duque and Barry Baxt*

Foot-and-Mouth Disease Research Unit, United States Department of Agriculture, Agricultural Research Service, Plum Island Animal Disease Center, Greenport, New York 11944-0848

Received 22 July 2002/ Accepted 14 November 2002

Three members of the {alpha}V integrin family of cellular receptors, {alpha}Vß1, {alpha}Vß3, and {alpha}Vß6, have been identified as receptors for foot-and-mouth disease virus (FMDV) in vitro. The virus interacts with these receptors via a highly conserved arginine-glycine-aspartic acid (RGD) amino acid sequence motif located within the ßG-ßH (G-H) loop of VP1. Other {alpha}V integrins, as well as several other integrins, recognize and bind to RGD motifs on their natural ligands and also may be candidate receptors for FMDV. To analyze the roles of the {alpha}V integrins from a susceptible species as viral receptors, we molecularly cloned the bovine ß1, ß5, and ß6 integrin subunits. Using these subunits, along with previously cloned bovine {alpha}V and ß3 subunits, in a transient expression assay system, we compared the efficiencies of infection mediated by {alpha}Vß1, {alpha}Vß3, {alpha}Vß5, and {alpha}Vß6 among three strains of FMDV serotype A and two strains of serotype O. While all the viruses could infect cells expressing these integrins, they exhibited different efficiencies of integrin utilization. All the type A viruses used {alpha}Vß3 and {alpha}Vß6 with relatively high efficiency, while only one virus utilized {alpha}Vß1 with moderate efficiency. In contrast, both type O viruses utilized {alpha}Vß6 and {alpha}Vß1 with higher efficiency than {alpha}Vß3. Only low levels of viral replication were detected in {alpha}Vß5-expressing cells infected with either serotype. Experiments in which the ligand-binding domains among the ß subunits were exchanged indicated that this region of the integrin subunit appears to contribute to the differences in integrin utilizations among strains. In contrast, the G-H loops of the different viruses do not appear to be involved in this phenomenon. Thus, the ability of the virus to utilize multiple integrins in vitro may be a reflection of the use of multiple receptors during the course of infection within the susceptible host.

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

Journal of Virology, February 2003, p. 2500-2511, Vol. 77, No. 4
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.4.2500-2511.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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