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Characterization of Hepatitis C virus intra- and intergenotypic chimeras reveals a role of the glycoprotein in virus envelopment

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Characterization of Hepatitis C virus intra- and intergenotypic chimeras reveals a role of the glycoprotein in virus envelopment

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dc.contributor.author Steinmann, Eike es_ES
dc.contributor.author Doerrbecker, Juliane es_ES
dc.contributor.author Friesland, Martina es_ES
dc.contributor.author Riebesehl, Nina es_ES
dc.contributor.author Ginkel, Corinne es_ES
dc.contributor.author Hillung, Julia es_ES
dc.contributor.author Gentzsch, Juliane es_ES
dc.contributor.author Lauber, Chris es_ES
dc.contributor.author Brown, Richard es_ES
dc.contributor.author Frentzen, Anne es_ES
dc.contributor.author Pietschmann, Thomas es_ES
dc.date.accessioned 2017-01-23T12:21:25Z
dc.date.available 2017-01-23T12:21:25Z
dc.date.issued 2013-12
dc.identifier.issn 0022-538X
dc.identifier.uri http://hdl.handle.net/10251/77223
dc.description.abstract [EN] Hepatitis C virus (HCV) is highly variable and associated with chronic liver disease. Viral isolates are grouped into seven genotypes (GTs). Accumulating evidence indicates that viral determinants in the core to NS2 proteins modulate the efficiency of virus production. However, the role of the glycoproteins E1 and E2 in this process is currently poorly defined. Therefore, we constructed chimeric viral genomes to explore the role of E1 and E2 in HCV assembly. Comparison of the kinetics and efficiency of particle production by intragenotypic chimeras highlighted core and p7 as crucial determinants for efficient virion release. Glycoprotein sequences, however, had only a minimal impact on this process. In contrast, in the context of intergenotypic HCV chimeras, HCV assembly was profoundly influenced by glycoprotein genes. On the one hand, insertion of GT1a-derived (H77) E1-E2 sequences into a chimeric GT2a virus (Jc1) strongly suppressed virus production. On the other hand, replacement of H77 glycoproteins within the GT1a-GT2a chimeric genome H77/C3 by GT2a-derived (Jc1) E1-E2 increased infectious particle production. Thus, within intergenotypic chimeras, glycoprotein features strongly modulate virus production. Replacement of Jc1 glycoprotein genes by H77-derived E1-E2 did not grossly affect subcellular localization of core, E2, and NS2. However, it caused an accumulation of nonenveloped core protein and increased abundance of nonenveloped core protein structures with slow sedimentation. These findings reveal an important role for the HCV glycoproteins E1 and E2 in membrane envelopment, which likely depends on a genotype-specific interplay with additional viral factors. es_ES
dc.description.sponsorship E.S. was supported by the DFG (STE 1954/1-1) and an intramural young investigator award of the Helmholtz Centre for Infection Research. T.P. was supported by grants from the DFG (PI 734/2-1) and the Helmholtz Association (SO-024).
dc.language Inglés es_ES
dc.publisher American Society for Microbiology es_ES
dc.relation.ispartof Journal of Virology es_ES
dc.rights Reserva de todos los derechos es_ES
dc.title Characterization of Hepatitis C virus intra- and intergenotypic chimeras reveals a role of the glycoprotein in virus envelopment es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1128/JVI.01708-13
dc.relation.projectID info:eu-repo/grantAgreement/DFG//STE 1954%2F1-1/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/DFG//PI 734%2F2-1/ es_ES
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes es_ES
dc.description.bibliographicCitation Steinmann, E.; Doerrbecker, J.; Friesland, M.; Riebesehl, N.; Ginkel, C.; Hillung, J.; Gentzsch, J.... (2013). Characterization of Hepatitis C virus intra- and intergenotypic chimeras reveals a role of the glycoprotein in virus envelopment. Journal of Virology. 87(24):13297-13306. https://doi.org/10.1128/JVI.01708-13 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://dx.doi.org/10.1128/JVI.01708-13 es_ES
dc.description.upvformatpinicio 13297 es_ES
dc.description.upvformatpfin 13306 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 87 es_ES
dc.description.issue 24 es_ES
dc.relation.senia 260607 es_ES
dc.identifier.pmcid PMC3838269 en_EN
dc.contributor.funder Deutsche Forschungsgemeinschaft


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