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Arginine-glycine-aspartic acid-specific binding by foot-and-mouth disease viruses to the purified integrin alpha(v)beta3 in vitro.

Abstract:

The integrin alpha(v)beta3 has been shown to act as the receptor for internalization of foot-and-mouth disease virus (FMDV) (A12), with attachment being through a highly conserved RGD motif located on the G-H loop of viral capsid protein VP1. In addition, however, we have recently shown that efficient infection of culture-grown cells by FMDV (O1BFS) requires binding to cell surface heparan sulfate. In this study, we have used a solid-phase receptor binding assay to characterize the binding by...

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Publication status:
Published

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Authors


Jackson, T More by this author
Ghazaleh, RA More by this author
Blakemore, WE More by this author
Ellard, FM More by this author
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Journal:
Journal of virology
Volume:
71
Issue:
11
Pages:
8357-8361
Publication date:
1997-11-05
EISSN:
1098-5514
ISSN:
0022-538X
URN:
uuid:4592b7e5-28b9-482e-a66c-2004e66f213b
Source identifiers:
4280
Local pid:
pubs:4280

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