Foot-and-mouth disease virus forms a highly stable, EDTA-resistant complex with its principal receptor, integrin alpha v beta 6: Implications for infectiousness

DiCara, Danielle and Burman, Alison and Clarke, Stuart J. and Berryman, Stephen and Howard, Mark J. and Hart, Ian R. and Marshall, John F. and Jackson, Terry (2008) Foot-and-mouth disease virus forms a highly stable, EDTA-resistant complex with its principal receptor, integrin alpha v beta 6: Implications for infectiousness. Journal of Virology, 82 (3). pp. 1537-1546. ISSN 0022-538X. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1128/JVI.01480-07

Abstract

The initial stage of foot-and-mouth disease virus (FMDV) infection is virus binding to cell surface integrins via the RGD motif in the GH loop of the VP1 capsid protein. As for all ligand/integrin interactions, the initial contact between FMDV and its integrin receptors is cation dependent and hence inhibited by EDTA. We have investigated this binding process with RGD-containing peptides derived from the VP1 capsid protein of FMDV and discovered that, upon binding, some of these peptides form highly stable, EDTA-resistant associations with integrin alpha v beta 6. Peptides containing specific substitutions show that this stable binding is dependent on a helical structure immediately C terminal to the RGD and, specifically, two leucine residues at positions RGD +1 and RGD +4. These observations have a biological consequence, as we show further that stable, EDTA-resistant binding to alpha v beta 6 is a property also exhibited by FMDV particles. Thus, the integrin-binding loop of FMDV appears to have evolved to form very stable complexes with the principal receptor of FMDV, integrin alpha v beta 6. An ability to induce such stable complexes with its cellular receptor is likely to contribute significantly to the high infectiousness of FMDV.

Item Type: Article
Additional information: 253JH Times Cited:0 Cited References Count:38 1098-5514 (Electronic) Journal Article Research Support, Non-U.S. Gov't
Uncontrolled keywords: major antigenic loop integrin alpha(v)beta(3) neutralizing antibody cell-adhesion binding alpha-v-beta-6 ligand spread fibronectin recognition
Subjects: Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Mark Howard
Date Deposited: 11 Mar 2009 15:37
Last Modified: 22 May 2014 14:05
Resource URI: http://kar.kent.ac.uk/id/eprint/5348 (The current URI for this page, for reference purposes)
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