Cryo-EM structure of Nipah virus RNA polymerase complex
Yiru Wang, Lixia Zhao, Yi Zhang, Yuhan Wang, Jiao Tang, Simiao Liu, Huihan Gao, Xiaoxiao Zhang, Luca Zinzula, Roger D. Kornberg, Heqiao Zhang
Abstract
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.