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.
Highlights
An effective interferon antagonist in human and avian cells, the novel H7N9 influenza virus NS1 protein is defective at inhibiting CPSF30
In agreement with our pulldown studies, NS1-L103F was unable to inhibit Renilla luciferase activity, while both NS1I106M and NS1-DM proteins efficiently limited activity (Fig. 2C). These results indicate that the single I106M substitution in H7N9 NS1 restores both CPSF30 binding and the inhibition of cellular gene expression
H7N9 NS1 is defective in binding CPSF30 and is unable to block host cell gene expression
Summary
An effective interferon antagonist in human and avian cells, the novel H7N9 influenza virus NS1 protein is defective at inhibiting CPSF30. A single I106M substitution in novel H7N9 NS1 enhances CPSF30 binding and inhibition of host gene expression.
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