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Tridimensional model structure and patterns of molecular evolution of Pepino mosaic virus TGBp3 protein

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Tridimensional model structure and patterns of molecular evolution of Pepino mosaic virus TGBp3 protein

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dc.contributor.author Hasiow-Jaroszewska, B es_ES
dc.contributor.author Czerwoniec, A es_ES
dc.contributor.author Pospieszny, H es_ES
dc.contributor.author Elena Fito, Santiago Fco es_ES
dc.date.accessioned 2017-05-18T11:56:44Z
dc.date.available 2017-05-18T11:56:44Z
dc.date.issued 2011-06-24
dc.identifier.issn 1743-422X
dc.identifier.uri http://hdl.handle.net/10251/81394
dc.description.abstract [EN] Background: Pepino mosaic virus (PepMV) is considered one of the most dangerous pathogens infecting tomatoes worldwide. The virus is highly diverse and four distinct genotypes, as well as inter-strain recombinants, have already been described. The isolates display a wide range on symptoms on infected plant species, ranging from mild mosaic to severe necrosis. However, little is known about the mechanisms and pattern of PepMV molecular evolution and about the role of individual proteins in host-pathogen interactions. Methods: The nucleotide sequences of the triple gene block 3 (TGB3) from PepMV isolates varying in symptomatology and geographic origin have been analyzed. The modes and patterns of molecular evolution of the TGBp3 protein were investigated by evaluating the selective constraints to which particular amino acid residues have been subjected during the course of diversification. The tridimensional structure of TGBp3 protein has been modeled de novo using the Rosetta algorithm. The correlation between symptoms development and location of specific amino acids residues was analyzed. Results: The results have shown that TGBp3 has been evolving mainly under the action of purifying selection operating on several amino acid sites, thus highlighting its functional role during PepMV infection. Interestingly, amino acid 67, which has been previously shown to be a necrosis determinant, was found to be under positive selection. Conclusions: Identification of diverse selection events in TGB3p3 will help unraveling its biological functions and is essential to an understanding of the evolutionary constraints exerted on the Potexvirus genome. The estimated tridimensional structure of TGBp3 will serve as a platform for further sequence, structural and function analysis and will stimulate new experimental advances. es_ES
dc.description.sponsorship This study was funded by the Polish Ministry of Science and Higher Education grants 0067/P01/2010/70 (AC) and N N310 163 438 and IP2010 012470 Iuventus Plus (to BHJ). The study was also supported by Foundation for Polish Science. Work in Valencia was supported by the Spanish MICINN grant BFU2009-06993 (to SFE) and by EMBO Short Term Fellowship ASTF424-2010 (to BHJ). en_EN
dc.language Inglés es_ES
dc.publisher BioMed Central es_ES
dc.relation.ispartof Virology Journal es_ES
dc.rights Reconocimiento (by) es_ES
dc.subject Molecular evolution es_ES
dc.subject PepMW es_ES
dc.subject Protein modeling es_ES
dc.subject Selective constraints es_ES
dc.subject TGBp3 es_ES
dc.subject Virus evolution es_ES
dc.title Tridimensional model structure and patterns of molecular evolution of Pepino mosaic virus TGBp3 protein es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1186/1743-422X-8-318
dc.relation.projectID info:eu-repo/grantAgreement/EC/FP7/263318/EU/How the brain codes the past to predict the future/ en_EN
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 Hasiow-Jaroszewska, B.; Czerwoniec, A.; Pospieszny, H.; Elena Fito, SF. (2011). Tridimensional model structure and patterns of molecular evolution of Pepino mosaic virus TGBp3 protein. Virology Journal. 8:1-8. https://doi.org/10.1186/1743-422X-8-318 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://doi.org/10.1186/1743-422X-8-318 es_ES
dc.description.upvformatpinicio 1 es_ES
dc.description.upvformatpfin 8 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 8 es_ES
dc.relation.senia 218187 es_ES
dc.identifier.pmid 21702943 en_EN
dc.identifier.pmcid PMC3132167
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