DiCara, D. and Burman, A. and Clark, S. and Berryman, S. and Howard, M.J. and Hart, I.R. and Marshall, J.F. and Jackson, T. (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.
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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.
|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:||14 Jan 2010 14:20|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/5348 (The current URI for this page, for reference purposes)|
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