A single amino acid substitution in the novel H7N9 influenza A virus NS1 protein increases CPSF30 binding and virulence.
A single amino acid substitution in the novel H7N9 influenza A virus NS1 protein increases CPSF30 binding and virulence.
复制标题
DOI：
10.1128/jvi.01567-14
复制
发表时间：
2014-10
影响因子：
5.4
通讯作者：
García-Sastre A
中科院分区：
文献类型：
--
作者：
Ayllon J;Domingues P;Rajsbaum R;Miorin L;Schmolke M;Hale BG;García-Sastre A
虽然在人和禽类细胞中是有效的干扰素拮抗剂，但新的H7N9流感病毒NS1蛋白在抑制CPSF30方面存在缺陷。H7N9 NS1中的I106M替换可以恢复CPSF30的结合并阻断宿主基因的表达。此外，表达H7N9 NS1-I106M的重组病毒在体内复制到更高的滴度，并且比亲本病毒的毒力略强。H7N9 NS1上增强CPSF30结合的自然多态可能是令人担忧的原因。
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.