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Contribution of NS1 effector domain dimerization to influenza A virus replication and virulence.

ABSTRACT: Conserved tryptophan-187 facilitates homodimerization of the influenza A virus NS1 protein effector domain. We generated a mutant influenza virus strain expressing NS1-W187R to destabilize this self-interaction. NS1-W187R protein exhibited lower double-stranded RNA (dsRNA)-binding activity, showed a temporal redistribution during infection, and was minimally compromised for interferon antagonism. The mutant virus replicated similarly to the wild type in vitro, but it was slightly attenuated for replication in mice, causing notably reduced morbidity and mortality. These data suggest biological relevance for the W187-mediated homotypic interaction of NS1.

SUBMITTER: Ayllon J 

PROVIDER: S-EPMC3497675 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Contribution of NS1 effector domain dimerization to influenza A virus replication and virulence.

Ayllon Juan J   Russell Rupert J RJ   García-Sastre Adolfo A   Hale Benjamin G BG  

Journal of virology 20120919 23

Conserved tryptophan-187 facilitates homodimerization of the influenza A virus NS1 protein effector domain. We generated a mutant influenza virus strain expressing NS1-W187R to destabilize this self-interaction. NS1-W187R protein exhibited lower double-stranded RNA (dsRNA)-binding activity, showed a temporal redistribution during infection, and was minimally compromised for interferon antagonism. The mutant virus replicated similarly to the wild type in vitro, but it was slightly attenuated for  ...[more]

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