tetano
Editor, Senior Moderator
J Virol. 2014 Jul 30. pii: JVI.01567-14. [Epub ahead of print]
A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence.
Ayllon J1, Domingues P2, Rajsbaum R1, Miorin L1, Schmolke M1, Hale BG3, Garc?a-Sastre A4.
Author information
Abstract
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 parental. Natural polymorphisms in H7N9 NS1 that enhance CPSF30 binding may be cause for concern.
Copyright ? 2014, American Society for Microbiology. All Rights Reserved.
PMID:
25078692
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25078692
A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence.
Ayllon J1, Domingues P2, Rajsbaum R1, Miorin L1, Schmolke M1, Hale BG3, Garc?a-Sastre A4.
Author information
Abstract
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 parental. Natural polymorphisms in H7N9 NS1 that enhance CPSF30 binding may be cause for concern.
Copyright ? 2014, American Society for Microbiology. All Rights Reserved.
PMID:
25078692
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25078692