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oai:riubu.ubu.es:10259/95282024-09-05T00:05:15Zcom_10259_4862com_10259_5086com_10259_2604col_10259_4863

2024-09-04T11:46:37Z urn:hdl:10259/9528 Contribution of NS1 Effector Domain Dimerization to Influenza A Virus Replication and Virulence Ayllón Barasoain, Juan Russell, Rupert J. García Sastre, Adolfo Hale, Benjamin G. 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. 2024-09-04T11:46:37Z 2024-09-04T11:46:37Z 2012-12 info:eu-repo/semantics/article 0022-538X http://hdl.handle.net/10259/9528 10.1128/jvi.02237-12 eng Journal of Virology. 2012, V. 86, n. 23, p. 13095–13098 https://doi.org/10.1128/jvi.02237-12 info:eu-repo/grantAgreement/NIH//R01AI04695/US/ info:eu-repo/grantAgreement/NIH//U19AI08302/US/ info:eu-repo/grantAgreement/NIAID//HHSN266200700010C/US/ info:eu-repo/grantAgreement/NCI//5R24 CA095823-04/US/ info:eu-repo/grantAgreement/NSF//DBI-9724504/US/ info:eu-repo/grantAgreement/NIH//1 S10 RR0 9145-01/US/ info:eu-repo/semantics/openAccess American Society for Microbiology