JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Neff, S.
Right arrow Articles by Baxt, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Neff, S.
Right arrow Articles by Baxt, B.

 Previous Article  |  Next Article 

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


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 2000 by the American Society for Microbiology. All rights reserved.