Cryo-EM structure of Nipah virus RNA polymerase complex
Yiru Wang1,2, Lixia Zhao1, Yi Zhang1
1Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 201210, Shanghai, China.
None:
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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