Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-1-18
pubmed:abstractText
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 alphavbeta6. 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 alphavbeta6 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 alphavbeta6. An ability to induce such stable complexes with its cellular receptor is likely to contribute significantly to the high infectiousness of FMDV.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-10069951, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-10799568, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-10982082, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-11040063, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-11773368, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-12230977, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-12527436, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-12527438, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-12527441, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-12859905, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-14754902, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-14960589, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-15078934, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-15858032, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-15893568, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-15956594, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-16186231, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-16517977, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-16973584, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-1717468, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-17244604, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-17374638, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-2077034, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-5270205, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-7064324, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-7533862, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-7537661, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-7846531, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-8042985, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-8120056, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-8131845, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-8385272, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-8454652, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-8662712, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-9343190, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-9353406, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-9557639, http://linkedlifedata.com/resource/pubmed/commentcorrection/18045932-9890954
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1098-5514
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
82
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1537-46
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Foot-and-mouth disease virus forms a highly stable, EDTA-resistant complex with its principal receptor, integrin alphavbeta6: implications for infectiousness.
pubmed:affiliation
Centre for Tumour Biology, Barts and the London Queen Mary's Medical and Dental School, Charterhouse Square, London EC1M 6BQ, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't