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TitleCryo-EM structure of Nipah virus RNA polymerase complex.
Journal, issue, pagesSci Adv, Vol. 10, Issue 50, Page eadr7116, Year 2024
Publish dateDec 13, 2024
AuthorsYiru Wang / Lixia Zhao / Yi Zhang / Yuhan Wang / Jiao Tang / Simiao Liu / Huihan Gao / Xiaoxiao Zhang / Luca Zinzula / Roger D Kornberg / Heqiao Zhang /
PubMed AbstractNipah virus, a member of the family, is a highly pathogenic nonsegmented, negative-sense RNA virus (nsNSV) which causes severe neurological and respiratory illnesses in humans. There are no ...Nipah virus, a member of the 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.
External linksSci Adv / PubMed:39661676 / PubMed Central
MethodsEM (single particle)
Resolution2.9 Å
Structure data

60355

8zpv

EMDB-60355, PDB-8zpv:
Nipah virus polymerase complex
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • henipavirus nipahense
KeywordsTRANSCRIPTION / polymerase / virus / Nipah

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