NS5的甲基转移酶和聚合酶之间的界面对于黄病毒复制至关重要。
The interface between methyltransferase and polymerase of NS5 is essential for flavivirus replication.
作者信息
Li Xiao-Dan, Shan Chao, Deng Cheng-Lin, Ye Han-Qing, Shi Pei-Yong, Yuan Zhi-Ming, Gong Peng, Zhang Bo
机构信息
CAS Key Laboratory of Special Pathogens and Biosafety, Center for Emerging Infectious Diseases, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China; University of Chinese Academy of Sciences, Beijing, China.
CAS Key Laboratory of Special Pathogens and Biosafety, Center for Emerging Infectious Diseases, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China; Key Laboratory of Agricultural and Environmental Microbiology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China.
出版信息
PLoS Negl Trop Dis. 2014 May 22;8(5):e2891. doi: 10.1371/journal.pntd.0002891. eCollection 2014 May.
The flavivirus NS5 harbors both a methyltransferase (MTase) and an RNA-dependent RNA polymerase (RdRP). Both enzyme activities of NS5 are critical for viral replication. Recently, the full-length NS5 crystal structure of Japanese encephalitis virus reveals a conserved MTase-RdRP interface that features two conserved components: a six-residue hydrophobic network and a GTR sequence. Here we showed for the first time that these key interface components are essential for flavivirus replication by various reverse genetics approaches. Interestingly, some replication-impaired variants generated a common compensatory NS5 mutation outside the interface (L322F), providing novel routes to further explore the crosstalk between MTase and RdRP.
黄病毒NS5蛋白兼具甲基转移酶（MTase）和RNA依赖的RNA聚合酶（RdRP）活性。NS5的这两种酶活性对于病毒复制至关重要。最近，日本脑炎病毒的全长NS5晶体结构揭示了一个保守的MTase-RdRP界面，该界面具有两个保守成分：一个六残基疏水网络和一个GTR序列。在此我们首次通过多种反向遗传学方法表明，这些关键的界面成分对于黄病毒复制至关重要。有趣的是，一些复制受损的变体在界面外产生了一个常见的补偿性NS5突变（L322F），为进一步探索MTase和RdRP之间的相互作用提供了新途径。
Zotero 插件