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Journal of Virology, August 2000, p. 7298-7306, Vol. 74, No. 16
0022-538X/00/$04.00+0

High-Efficiency Utilization of the Bovine Integrin alpha vbeta 3 as a Receptor for Foot-and-Mouth Disease Virus Is Dependent on the Bovine beta 3 Subunit

Sherry Neff, Peter W. Mason, and Barry Baxt*

Foot-and-Mouth Disease Research Unit, USDA Agricultural Research Service, Plum Island Animal Disease Center, Greenport, New York 11944

Received 6 March 2000/Accepted 19 May 2000

We have previously reported that Foot-and-mouth disease virus (FMDV), which is virulent for cattle and swine, can utilize the integrin alpha vbeta 3 as a receptor on cultured cells. Since those studies were performed with the human integrin, we have molecularly cloned the bovine homolog of the integrin alpha vbeta 3 and have compared the two receptors for utilization by FMDV. Both the alpha v and beta 3 subunits of the bovine integrin have high degrees of amino acid sequence similarity to their corresponding human subunits in the ectodomains (96%) and essentially identical transmembrane and cytoplasmic domains. Within the putative ligand-binding domains, the bovine and human alpha v subunits have a 98.8% amino acid sequence similarity while there is only a 93% similarity between the beta 3 subunits of these two species. COS cell cultures, which are not susceptible to FMDV infection, become susceptible if cotransfected with alpha v and beta 3 subunit cDNAs from a bovine or human source. Cultures cotransfected with the bovine alpha vbeta 3 subunit cDNAs and infected with FMDV synthesize greater amounts of viral proteins than do infected cultures cotransfected with the human integrin subunits. Cells cotransfected with a bovine alpha v subunit and a human beta 3 subunit synthesize viral proteins at levels equivalent to those in cells expressing both human subunits. However, cells cotransfected with the human alpha v and the bovine beta 3 subunits synthesize amounts of viral proteins equivalent to those in cells expressing both bovine subunits, indicating that the bovine beta 3 subunit is responsible for the increased effectiveness of this receptor. By engineering chimeric bovine-human beta 3 subunits, we have shown that this increase in receptor efficiency is due to sequences encoding the C-terminal one-third of the subunit ectodomain, which contains a highly structured cysteine-rich repeat region. We postulate that amino acid sequence differences within this region may be responsible for structural differences between the human and bovine beta 3 subunit, leading to more efficient utilization of the bovine receptor by this bovine pathogen.

* 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) 323-2507. E-mail: bbaxt{at}piadc.ars.usda.gov.

Journal of Virology, August 2000, p. 7298-7306, Vol. 74, No. 16
0022-538X/00/$04.00+0


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