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Scientific article
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English

A single amino acid substitution in the novel H7N9 influenza A virus NS1 protein increases CPSF30 binding and virulence

Contributors

Ayllon, Juan; Domingues, Patricia; Rajsbaum, Ricardo; Miorin, Lisa; Schmolke, Mirco; Hale, Benjamin G; García-Sastre, Adolfo

Published in

Journal of virology, vol. 88, no. 20, p. 12146-12151

Publication date

2014

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 the parental virus. Natural polymorphisms in H7N9 NS1 that enhance CPSF30 binding may be cause for concern.

Keywords

  • Amino Acid Substitution
  • Amino Acids/genetics
  • Animals
  • Chickens
  • Gene Expression
  • Humans
  • Influenza A Virus, H7N9 Subtype/metabolism/pathogenicity/physiology
  • Viral Nonstructural Proteins/genetics/metabolism
  • Viral Proteins/metabolism
  • Virulence

UNIGE affiliation entities

Not a UNIGE publication

Citation (ISO format)

AYLLON, Juan et al. A single amino acid substitution in the novel H7N9 influenza A virus NS1 protein increases CPSF30 binding and virulence. In: Journal of virology, 2014, vol. 88, n° 20, p. 12146–12151. doi: 10.1128/JVI.01567-14

Main files (1)

Article (Published version)

Identifiers

Journal ISSN

0022-538X
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Technical informations

Creation

17/09/2015 15:03:00

First validation

17/09/2015 15:03:00

Update

14/03/2023 23:44:40

Status update

14/03/2023 23:44:39

Last indexation

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