Cryo-EM structure of Nipah virus RNA polymerase complex

文献类型： 外文期刊

第一作者： Wang, Yiru

作者： Wang, Yiru;Zhao, Lixia;Zhang, Yi;Gao, Huihan;Kornberg, Roger D.;Zhang, Heqiao;Wang, Yiru;Wang, Yuhan;Gao, Huihan;Wang, Yuhan;Zhang, Xiaoxiao;Zinzula, Luca;Tang, Jiao;Liu, Simiao;Kornberg, Roger D.

作者机构：

期刊名称：SCIENCE ADVANCES （ 影响因子：12.5； 五年影响因子：14.1 ）

ISSN： 2375-2548

年卷期： 2024 年 10 卷 50 期

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收录情况： SCI

摘要： Nipah virus, a member of the Paramyxoviridae family, is a highly pathogenic nonsegmented, negative-sense RNA virus (nsNSV) which causes severe neurological and respiratory illnesses in humans. There are no available drugs or vaccines to combat this virus. A complex of large polymerase protein (L) and phosphoprotein (P) of Nipah virus supports replication and transcription and affords a target for antiviral drug development. Structural information required for drug development is lacking. Here we report the 2.9-angstrom cryo-electron microscopy structure of the Nipah virus polymerase-phosphoprotein complex. The structure identifies conserved amino acids likely important for recognition of template RNA by nsNSVs and reveals the locations of mutation-prone sites among Nipah virus strains, which may facilitate the development of therapeutic agents against Nipah virus by targeting regions unaffected by these mutation sites.

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