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Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.advisor | Gutiérrez-Escolano, Ana Lorena | - |
dc.contributor.author | Cancio-Lonches, Clotilde | - |
dc.contributor.author | Yocupicio-Monroy, Martha | - |
dc.contributor.author | Sandoval-Jaime, Carlos | - |
dc.contributor.author | Galván-Mendoza, Iván | - |
dc.contributor.author | Ureña, Luis | - |
dc.contributor.author | Vashist, Surender | - |
dc.contributor.author | Goodfellow, Ian | - |
dc.contributor.author | Salas-Benito, Juan Santiago | - |
dc.contributor.author | Gutiérrez-Escolano, Ana Lorena | - |
dc.date.accessioned | 2012-10-16T23:08:25Z | - |
dc.date.available | 2012-10-16T23:08:25Z | - |
dc.date.issued | 2011-08 | - |
dc.identifier.citation | Cancio-Lonches C, Yocupicio-Monroy M, Sandoval-Jaime C, Galván-Mendoza I, Ureña L, Vashist S, Goodfellow I, Salas-Benito J, Gutiérrez-Escolano AL. Nucleolin interacts with the Feline calicivirus 3’ untranslate region and the protease-polymerase NS6 and NS7 proteins, playing a role in virus replication. J Virol. 2011. 85(16): 8056-8068. | es |
dc.identifier.issn | 0022-538X | - |
dc.identifier.uri | http://www.repositoriodigital.ipn.mx/handle/123456789/7311 | - |
dc.description | Artículo científico | es |
dc.description.abstract | Cellular proteins play many important roles during the life cycle of all viruses. Specifically, host cell nucleic acid-binding proteins interact with viral components of positive-stranded RNA viruses and regulate viral translation, as well as RNA replication. Here, we report that nucleolin, a ubiquitous multifunctional nucleolar shuttling phosphoprotein, interacts with the Norwalk virus and feline calicivirus (FCV) genomic 3 untranslated regions (UTRs). Nucleolin can also form a complex in vitro with recombinant Norwalk virus NS6 and -7 (NS6/7) and can be copurified with the analogous protein from feline calicivirus (p76 or NS6/7) from infected feline kidney cells. Nucleolin RNA levels or protein were not modified during FCV infection; however, as a consequence of the infection, nucleolin was seen to relocalize from the nucleoli to the nucleoplasm, as well as to the perinuclear area where it colocalizes with the feline calicivirus NS6/7 protein. In addition, antibodies to nucleolin were able to precipitate viral RNA from feline calicivirus-infected cells, indicating a direct or indirect association of nucleolin with the viral RNA during virus replication. Small interfering RNA (siRNA)-mediated knockdown of nucleolin resulted in a reduction of the cytopathic effect and virus yield in CrFK cells. Taken together, these results demonstrate that nucleolin is a nucleolar component that interacts with viral RNA and NS6/7 and is required for feline calicivirus replication | es |
dc.description.sponsorship | 43788-Q from Consejo Nacional de Ciencia y Tecnología and ICYTDF/247 from Instituto de Ciencia y Tecnología del Distrito Federal, Me´xico, D. F., to A.L.G.-E. and by a grant from the Wellcome Trust to I.G. I.G. is a Wellcome Trust Senior Fellow. | es |
dc.language.iso | en | es |
dc.publisher | Journal of Virology | es |
dc.subject | Calicivirus | es |
dc.subject | Nucleolina | es |
dc.subject | Replicación | es |
dc.subject | Transporte nuclear | es |
dc.subject | Proteasa-polimerasa | es |
dc.title | Nucleolin interacts with the Feline calicivirus 3’ untranslate region and the protease-polymerase NS6 and NS7 proteins, playing a role in virus replication | es |
dc.type | Article | es |
dc.description.especialidad | Medicina | es |
dc.description.tipo | 13 páginas | es |
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