Post-translational regulation of rotavirus protein NSP1 expression in mammalian cells

C. Piña-Vázquez, M. De Nova-Ocampo, S. Guzmán-León, L. Padilla-Noriega

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The nonstructural rotavirus protein NSP1 binds specifically to viral mRNAs and to interferon regulatory factor 3 (IRF3), inducing IRF3 degradation through a proteasome-dependent pathway. By using a vaccinia virus expression system in mammalian cells, we found that the yield of NSP1 was 8- and 13-fold lower than the viral proteins VP2 or NSP3, respectively; while in the presence of proteasome inhibitors such difference could be reduced to 2- to 2.5-fold, respectively. The susceptibility of NSP1 to proteasome degradation was fully reversed in a dose-dependent manner by transfection with the full complement of 11 molecules of translation-competent rotavirus mRNAs, but this effect was abrogated by the protein synthesis inhibitor cycloheximide. These results demonstrate that NSP1 is degraded through a proteasome-dependent pathway, and viral proteins, alone or in combination with viral mRNAs, interfere with such degradation. © 2006 Springer-Verlag.
Original languageAmerican English
Pages (from-to)345-368
Number of pages308
JournalArchives of Virology
DOIs
StatePublished - 1 Feb 2007
Externally publishedYes

Fingerprint

Proteasome Endopeptidase Complex
Interferon Regulatory Factor-3
Viral Proteins
Messenger RNA
Proteasome Inhibitors
Protein Synthesis Inhibitors
Vaccinia virus
Rotavirus
Cycloheximide
Transfection
Rotavirus NSP1 protein

Cite this

Piña-Vázquez, C. ; De Nova-Ocampo, M. ; Guzmán-León, S. ; Padilla-Noriega, L. / Post-translational regulation of rotavirus protein NSP1 expression in mammalian cells. In: Archives of Virology. 2007 ; pp. 345-368.
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Post-translational regulation of rotavirus protein NSP1 expression in mammalian cells. / Piña-Vázquez, C.; De Nova-Ocampo, M.; Guzmán-León, S.; Padilla-Noriega, L.

In: Archives of Virology, 01.02.2007, p. 345-368.

Research output: Contribution to journalArticle

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