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Title

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

Authors
Ayllon, Juan
Domingues, Patricia
Rajsbaum, Ricardo
Miorin, Lisa
Hale, Benjamin G
García-Sastre, Adolfo
Published in Journal of Virology. 2014, vol. 88, no. 20, p. 12146-12151
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 SubstitutionAmino Acids/geneticsAnimalsChickensGene ExpressionHumansInfluenza A Virus, H7N9 Subtype/metabolism/pathogenicity/physiologyViral Nonstructural Proteins/genetics/metabolismViral Proteins/metabolismVirulence
Identifiers
PMID: 25078692
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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. https://archive-ouverte.unige.ch/unige:76387

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Deposited on : 2015-10-22

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