2026-11-01T23:40:17Zhttps://riubu.ubu.es/oai/requestoai:riubu.ubu.es:10259/95282024-09-05T00:05:15Zcom_10259_4862com_10259_5086com_10259_2604col_10259_4863
Repositorio Institucional de la Universidad de Burgos
author
Ayllón Barasoain, Juan
author
Russell, Rupert J.
author
García Sastre, Adolfo
author
Hale, Benjamin G.
2024-09-04T11:46:37Z
2024-09-04T11:46:37Z
2012-12
0022-538X
http://hdl.handle.net/10259/9528
10.1128/jvi.02237-12
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.
eng
Contribution of NS1 Effector Domain Dimerization to Influenza A Virus Replication and Virulence
info:eu-repo/semantics/article
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URL
https://riubu.ubu.es/bitstream/10259/9528/1/Ayllon-jv_2012-2.pdf
File
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Ayllon-jv_2012-2.pdf