Cryo-EM structure of Nipah virus RNA polymerase complex

Nipah virus, a member of the <i>Paramyxoviridae</i> 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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Publication Details

Journal
Science Advances
Published
2024-12-11
DOI
https://doi.org/10.1126/sciadv.adr7116
Citations
10
Primary Topic
Virology and Viral Diseases
Type
article
Field-Weighted Citation Impact
3.87

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Cryo-EM structure of Nipah virus RNA polymerase complex

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10 citations
Science Advances
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article

Cryo-EM structure of Nipah virus RNA polymerase complex

Heqiao Zhang, Huihan Gao, Roger D. Kornberg, Luca Zinzula, Simiao Liu, Xiaoxiao Zhang, Jiao Tang, Yi Zhang, Yuhan Wang, Lixia Zhao, Yiru Wang
article en
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Abstract

Nipah virus, a member of the <i>Paramyxoviridae</i> 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.

Science AdvancesVol. 10(50)
Chinese Academy of Sciences (CN), ShanghaiTech University (CN), State Key Laboratory of Plant Genomics (CN), Institute of Genetics and Developmental Biology (CN), Chinese Academy of Agricultural Sciences (CN), Institute of Apiculture Research (CN), Stanford University (US)
ShanghaiTech University
Good health and well-being
Openalex Percentile: Top 6%
Virology and Viral Diseases
3.87
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