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The N-terminal residual arginine19 of influenza A virus NS1 protein is required for its nuclear localization and RNA binding
Veterinary Microbiology ( IF 2.4 ) Pub Date : 2020-10-14 , DOI: 10.1016/j.vetmic.2020.108895
Xingbo Wang 1 , Lulu Lin 1 , Yang Yu 1 , Yan Yan 1 , Nishant Kumar Ojha 1 , Jiyong Zhou 2
Affiliation  

RNA binding ability and cellular distribution are important for nonstructural protein 1 (NS1) of influenza A virus to act as a viral regulatory factor to control virus life cycle. In this study, we identified that the N-terminal residues 19−21 of NS1 are a highly conserved motif depending on all the available NS1 full length sequence of H5N1 influenza A virus from NCBI database. Site-directed mutation analysis demonstrated that the R19 residue of NS1 is critical for its RNA binding and nuclear localization. Furthermore, the residue R19 of NS1 was identified to be critical for regulating M1 mRNA splicing and NS1 nuclear export. Biological analysis of the rescued viruses indicated that the R19A mutation of NS1 did not interfere the replication of H5N1 virus during infection and attenuated the virulence of H5N1 virus in mice.



中文翻译:

甲型流感病毒NS1蛋白的N末端残留精氨酸19是其核定位和RNA结合所必需的

RNA结合能力和细胞分布对于甲型流感病毒的非结构蛋白1(NS1)起到控制病毒生命周期的病毒调节因子的作用很重要。在这项研究中,我们确定了NS1的N末端残基19-21是高度保守的基序,这取决于从NCBI数据库获得的H5N1甲型流感病毒的所有可用NS1全长序列。定点突变分析表明,NS1的R 19残基对于其RNA结合和核定位至关重要。此外,NS1的残基R 19被确定对于调节M1 mRNA剪接和NS1核输出至关重要。对获救病毒的生物学分析表明,R 19NS1的突变不会在感染过程中干扰H5N1病毒的复制,并减弱了小鼠中H5N1病毒的毒力。

更新日期:2020-10-30
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