2026-06-29T21:02:00Zhttps://riubu.ubu.es/oai/request

oai:riubu.ubu.es:10259/79952023-11-23T12:25:10Zcom_10259_4862com_10259_5086com_10259_2604col_10259_4863

Ayllón Barasoain, Juan Domingues, Patricia Rajsbaum, Ricardo Miorin, Lisa Schmolke, Mirco Hale, Benjamin G. García Sastre, Adolfo 2023-11-13T08:05:36Z 2023-11-13T08:05:36Z 2014 0022-538X http://hdl.handle.net/10259/7995 10.1128/JVI.01567-14 1098-5514 Although an effective interferon antagonist in human and avian cells, the novel H7N9 influenza virus NS1 protein is defective at inhibiting CPSF30. An I106M substitution in H7N9 NS1 can restore CPSF30 binding together with the ability to block host gene expression. Furthermore, a recombinant virus expressing H7N9 NS1-I106M replicates to higher titers in vivo, and is subtly more virulent, than the parental virus. Natural polymorphisms in H7N9 NS1 that enhance CPSF30 binding may be cause for concern. eng http://creativecommons.org/licenses/by/3.0/ info:eu-repo/semantics/openAccess Attribution 3.0 Unported A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence info:eu-repo/semantics/article