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dc.contributor.authorBaranowski, Eric-
dc.contributor.authorSevilla, Noemí-
dc.contributor.authorVerdaguer, Núria-
dc.contributor.authorRuiz-Jarabo, Carmen M.-
dc.contributor.authorBeck, Ewald-
dc.contributor.authorDomingo, Esteban-
dc.date.accessioned2008-11-13T15:27:58Z-
dc.date.available2008-11-13T15:27:58Z-
dc.date.issued1998-
dc.identifier.citationJournal of Virology 72(8): 6362-6372 (1998)en_US
dc.identifier.issn0022-538X-
dc.identifier.urihttp://hdl.handle.net/10261/8550-
dc.description.abstractHypervirulent variants of foot-and-mouth disease virus (FMDV) of serotype C arise upon serial cytolytic or persistent infections in cell culture. A specific mutation in the internal ribosome entry site of persistent FMDV was previously associated with enhanced translation initiation activity that could contribute to the hypervirulent phenotype for BHK-21 cells. Here we report that several hypervirulent FMDV variants arising upon serial cytolytic passage show an invariant internal ribosome entry site but have a number of mutations affecting structural and nonstructural viral proteins. The construction of chimeric type O-type C infectious transcripts has allowed the mapping of a major determinant of hypervirulence to the viral capsid. Tissue culture-adapted FMDV displayed enhanced affinity for heparin, but binding to cell surface heparan sulfate moieties was not required for expression of the hypervirulent phenotype in Chinese hamster ovary (CHO) cells. Virulence was identical or even higher for glycosaminoglycan-deficient CHO cells than for wild-type CHO cells. FMDV variants with decreased affinity for heparin were selected from a high-binding parental population and analyzed. Substitutions associated with decreased heparin binding were located at positions 173 of capsid protein VP3 and 144 of capsid protein VP1. These substitutions had a moderate effect on virulence for BHK-21 cells but completely abrogated infection of CHO cells. The comparative results with several FMDV isolates show that (i) increased affinity for heparin and alterations in cell tropism may be mediated by a number of independent sites on the viral capsid and (ii) the same capsid modifications may have different effects on different cell typesen_US
dc.description.sponsorshipWork in Madrid was supported by grant PB94-0034-C02-01 from DGICYT and Fundación Ramón Areces. Work at CID in Barcelona was supported by grant PB 95-0218 from DGICYT. Work in Giessen was supported by grant SFB 535 from Deutsche Forschungsgemeinschaften_US
dc.format.extent515935 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.titleMultiple virulence determinants of foot-and-mouth disease virus in cell cultureen_US
dc.typeartículoen_US
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://jvi.asm.org/cgi/content/full/72/8/6362en_US
dc.identifier.e-issn1098-5514-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.contributor.funderFundación Ramón Areces-
dc.contributor.funderGerman Research Foundation-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/100008054es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100001659es_ES
dc.identifier.pmid9658076-
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