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dc.contributor.author | Riolobos, Laura | - |
dc.contributor.author | Valle, Noelia | - |
dc.contributor.author | Hernando, Eva | - |
dc.contributor.author | Maroto, Beatriz | - |
dc.contributor.author | Kann, Michael | - |
dc.contributor.author | Almendral, José M. | - |
dc.date.accessioned | 2013-06-14T08:29:29Z | - |
dc.date.available | 2013-06-14T08:29:29Z | - |
dc.date.issued | 2010 | - |
dc.identifier | doi: 10.1128/JVI.01550-09 | - |
dc.identifier | issn: 0022-538X | - |
dc.identifier | e-issn: 1098-5514 | - |
dc.identifier.citation | Journal of Virology 84(4): 2090-2099 (2010) | - |
dc.identifier.uri | http://hdl.handle.net/10261/78134 | - |
dc.description.abstract | The central role of Raf protein kinase isoforms in human cancer demands specific anti-Raf therapeutic inhibitors. Parvoviruses are currently used in experimental cancer therapy due to their natural oncotropism and lytic life cycle. In searching for mechanisms underlying parvovirus oncolysis, we found that trimers of the major structural protein (VP) of the parvovirus minute virus of mice (MVM), which have to be imported into the nucleus for capsid assembly, undergo phosphorylation by the Raf-1 kinase. Purified Raf-1 phosphorylated the capsid subunits in vitro to the two-dimensional pattern found in natural MVM infections. VP trimers isolated from mammalian cells translocated into the nucleus of digitonin-permeabilized human cells. In contrast, VP trimers isolated from insect cells, which are devoid of Raf-1, were neither phosphorylated nor imported into the mammalian nucleus. However, the coexpression of a constitutively active Raf-1 kinase in insect cells restored VP trimer phosphorylation and nuclear transport competence. In MVM-infected normal and transformed cells, Raf-1 inhibition resulted in cytoplasmic retention of capsid proteins, preventing their nuclear assembly and progeny virus maturation. The level of Raf-1 activity in cancer cells was consistent with the extent of VP specific phosphorylation and with the permissiveness to MVM infection. Thus, Raf-1 control of nuclear translocation of MVM capsid assembly intermediates provides a novel target for viral oncolysis. MVM may reinforce specific therapies against frequent human cancers with deregulated Raf signaling. © 2010, American Society for Microbiology. All Rights Reserved. | - |
dc.description.sponsorship | This study was supported by grants from the Spanish Ministerio de Ciencia e Innovación (SAF2008-03238) and Comunidad de Madrid (S-SAL/0185/2006) to the laboratory of J.M.A. and by an institutional grant from Fundación Ramón Areces to the Centro de Biología Molecular “Severo Ochoa.” L.R. was supported in part by a short-term EMBO fellowship. | - |
dc.language.iso | eng | - |
dc.publisher | American Society for Microbiology | - |
dc.rights | openAccess | - |
dc.title | Viral oncolysis that targets raf-1 signaling control of nuclear transport | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1128/JVI.01550-09 | - |
dc.relation.publisherversion | http://dx.doi.org/10.1128/JVI.01550-09 | - |
dc.date.updated | 2013-06-14T08:29:30Z | - |
dc.description.version | Peer Reviewed | - |
dc.contributor.funder | Ministerio de Ciencia e Innovación (España) | - |
dc.contributor.funder | Comunidad de Madrid | - |
dc.contributor.funder | Fundación Ramón Areces | - |
dc.contributor.funder | EMBO | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100004837 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100008054 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003043 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100012818 | es_ES |
dc.identifier.pmid | 19939915 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | open | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | With Fulltext | - |
item.languageiso639-1 | en | - |
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Viral Oncolysis.pdf | 1,4 MB | Adobe PDF | Visualizar/Abrir |
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