Phosphorylation Generates Different Forms of Rotavirus NSP5

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Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2.

We have previously shown that a number of isoforms of the non-structural rotavirus protein NSP5 are found in virus-infected cells. These isoforms differ in their level of phosphorylation which, at least in part, appears to occur through autophosphorylation. NSP5 co-localizes with another non-structural protein, NSP2, in the viroplasms of infected cells where virus replication takes place. We no...

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In vivo and in vitro phosphorylation of rotavirus NSP5 correlates with its localization in viroplasms.

NSP5 (NS26), the product of rotavirus gene 11, is a phosphoprotein whose role in the virus replication cycle is unknown. To gain further insight into its function, we obtained monoclonal antibodies against the baculovirus-expressed protein. By immunoprecipitation and immunoblotting experiments, we showed that (i) NSP5 appears in many different phosphorylated forms in rotavirus-infected cells; (...

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Association of rotavirus viroplasms with microtubules through NSP2 and NSP5.

Rotavirus replication and virus assembly take place in electrodense spherical structures known as viroplasms whose main components are the viral proteins NSP2 and NSP5. The viroplasms are produced since early times after infection and seem to grow by stepwise addition of viral proteins and by fusion, however, the mechanism of viropIasms formation is unknown. In this study we found that the viro...

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Rotavirus nonstructural protein NSP5 interacts with major core protein VP2.

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ژورنال

عنوان ژورنال: Journal of General Virology

سال: 1996

ISSN: 0022-1317,1465-2099

DOI: 10.1099/0022-1317-77-9-2059