Mañana, JUEVES, 24 DE ABRIL, el sistema se apagará debido a tareas habituales de mantenimiento a partir de las 9 de la mañana. Lamentamos las molestias.
Impact of vesicular stomatitis virus M proteins on different cellular functions
Entity
UAM. Departamento de Biología MolecularPublisher
Public Library of ScienceDate
2015-06-19Citation
10.1371/journal.pone.0131137
PLoS ONE 10.6 (2015): e0131137
ISSN
1932-6203 (print)DOI
10.1371/journal.pone.0131137Funded by
This study was supported by a DGICYT (Dirección General de Investigación Científica y Técnica. Ministerio de Economía y Competitividad, Spain) grant (BFU2012-31861). The Institutional Grant awarded to the Centro de Biología Molecular “Severo Ochoa” (CSIC-UAM) by the Fundación Ramón Areces is acknowledgedEditor's Version
http://dx.doi.org/10.1371/journal.pone.0131137Subjects
Cell membrane permeability; Cytoplasm; RNA splicing; Vesiculovirus; Virus cell interaction; Biología y Biomedicina / BiologíaRights
© 2015 Redondo et al.Abstract
Three different matrix (M) proteins termed M1, M2 and M3 have been described in cells infected with vesicular stomatitis virus (VSV). Individual expression of VSV M proteins induces an evident cytopathic effect including cell rounding and detachment, in addition to a partial inhibition of cellular protein synthesis, likely mediated by an indirect mechanism. Analogous to viroporins, M1 promotes the budding of new virus particles; however, this process does not produce an increase in plasma membrane permeability. In contrast to M1, M2 and M3 neither interact with the cellular membrane nor promote the budding of double membrane vesicles at the cell surface. Nonetheless, all three species of M protein interfere with the transport of cellular mRNAs from the nucleus to the cytoplasm and also modulate the redistribution of the splicing factor. The present findings indicate that all three VSV M proteins share some activities that interfere with host cell functions
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Google Scholar:Redondo, Natalia
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Madan, Vanesa
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Alvarez, Enrique
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Carrasco, Luis
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