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dc.contributor.authorBaranowski, Eric-
dc.contributor.authorRuiz-Jarabo, Carmen M.-
dc.contributor.authorSevilla, Noemí-
dc.contributor.authorAndreu, David-
dc.contributor.authorBeck, Ewald-
dc.contributor.authorDomingo, Esteban-
dc.date.accessioned2008-11-13T15:19:55Z-
dc.date.available2008-11-13T15:19:55Z-
dc.date.issued2000-
dc.identifier.citationJournal of Virology, 2000, p. 1641-1647, Vol. 74, No. 4en_US
dc.identifier.issn0022-538X-
dc.identifier.urihttp://hdl.handle.net/10261/8549-
dc.description.abstractCell surface molecules that can act as virus receptors may exert an important selective pressure on RNA viral quasispecies. Large population passages of foot-and-mouth disease virus (FMDV) in cell culture select for mutant viruses that render dispensable a highly conserved Arg-Gly-Asp (RGD) motif responsible for integrin receptor recognition. Here, we provide evidence that viability of recombinant FMDVs including a Asp-143Gly change at the RGD motif was conditioned by a number of capsid substitutions selected upon FMDV evolution in cell culture. Multiply passaged FMDVs acquired the ability to infect human K-562 cells, which do not express integrin alpha-v-beta-3. In contrast to previously described cell culture-adapted FMDVs, the RGD-independent infection did not require binding to the surface glycosaminoglycan heparan sulfate (HS). Viruses which do not bind HS and lack the RGD integrin-binding motif replicate efficiently in BHK-21 cells. Interestingly, FMDV mutants selected from the quasispecies for the inability to bind heparin regained sensitivity to inhibition by a synthetic peptide that represents the G-H loop of VP1. Thus, a single amino acid replacement leading to loss of HS recognition can shift preferential receptor usage of FMDV from HS to integrin. These results indicate at least three different mechanisms for cell recognition by FMDV and suggest a potential for this virus to use multiple, alternative receptors for entry even into the same cell typeen_US
dc.description.sponsorshipWork in Madrid was supported by grants PM 97-0060-C02-01, FAIR 5PL97-3665, and Fundación Ramón Areces. E.Baranowski was supported by a postdoctoral fellowship from Ministerio de Educación y Cultura, and C.R.-J. was supported by a fellowship from Comunidad Autónoma de Madrid. Work in Barcelona was supported by grant PB97-0873. A visit of E.Baranowski to Plum Island Animal Disease Center was supported by a fellowship under the OECD Co-Operative Research Programme: Biological Resource Management for Sustainable Agricultural Systemsen_US
dc.format.extent121551 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.publisherAmerican Society for Microbiologyen_US
dc.rightsopenAccessen_US
dc.subjectFoot-and-mouth disease virusen_US
dc.titleCell recognition by foot-and-mouth disease virus that lacks the RGD integrin-binding motif: blexibility in aphthovirus receptor usageen_US
dc.typeArtículoen_US
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://jvi.asm.org/cgi/content/full/74/4/1641en_US
dc.identifier.e-issn1098-5514-
dc.contributor.funderFundación Ramón Areces-
dc.contributor.funderMinisterio de Educación y Cultura (España)-
dc.contributor.funderComunidad de Madrid-
dc.identifier.funderhttp://dx.doi.org/10.13039/100008054es_ES
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