NS1-BINDING PROTEIN (NS1-BP) - A NOVEL HUMAN PROTEIN THAT INTERACTS WITH THE INFLUENZA-A VIRUS NONSTRUCTURAL NS1 PROTEIN IS RELOCALIZED IN THE NUCLEI OF INFECTED-CELLS

Citation
T. Wolff et al., NS1-BINDING PROTEIN (NS1-BP) - A NOVEL HUMAN PROTEIN THAT INTERACTS WITH THE INFLUENZA-A VIRUS NONSTRUCTURAL NS1 PROTEIN IS RELOCALIZED IN THE NUCLEI OF INFECTED-CELLS, Journal of virology, 72(9), 1998, pp. 7170-7180
Citations number
77
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Virology
Journal title
ISSN journal
0022-538X
Volume
72
Issue
9
Year of publication
1998
Pages
7170 - 7180
Database
ISI
SICI code
0022-538X(1998)72:9<7170:NP(-AN>2.0.ZU;2-1
Abstract
We used the yeast interaction trap system to identify a novel human 70 -kDa protein, termed NS1-binding protein (NS1-BP), which interacts wit h the nonstructural NS1 protein of the influenza A virus. The genetic interaction was confirmed by the specific coprecipitation of the NS1 p rotein from solution by a glutathione S-transferase-NS1-BP fusion prot ein and glutathione-Sepharose. NS1-BP contains an N-terminal BTB/POZ d omain and five kelch-like tandem repeat elements of similar to 50 amin o acids. In noninfected cells, affinity-purified antibodies localized NS1-BP in nuclear regions enriched with the spliceosome assembly facto r SC35, suggesting an association of NS1-BP with the cellular splicing apparatus. In influenza A virus-infected cells, NS1-BP relocalized th roughout the nucleoplasm and appeared distinct from the SC35 domains, which suggests that NS1-BP function may be disturbed or altered. The a ddition of a truncated NS1-BP mutant protein to a HeLa cell nuclear ex tract efficiently inhibited pre-mRNA splicing but not spliceosome asse mbly, This result could be explained by a possible dominant-negative e ffect of the NS1-BP mutant protein and suggests a role of the wild-typ e NS1-BP in promoting pre-mRNA splicing. These data suggest that the i nhibition of splicing by the NS1 protein may be mediated by binding to NS1-BP.