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TitleStructural and functional analysis of the Nipah virus polymerase complex.
Journal, issue, pagesCell, Vol. 188, Issue 3, Page 688-703.e18, Year 2025
Publish dateFeb 6, 2025
AuthorsSide Hu / Heesu Kim / Pan Yang / Zishuo Yu / Barbara Ludeke / Shawna Mobilia / Junhua Pan / Margaret Stratton / Yuemin Bian / Rachel Fearns / Jonathan Abraham /
PubMed AbstractNipah virus (NiV) is a bat-borne, zoonotic RNA virus that is highly pathogenic in humans. The NiV polymerase, which mediates viral genome replication and mRNA transcription, is a promising drug ...Nipah virus (NiV) is a bat-borne, zoonotic RNA virus that is highly pathogenic in humans. The NiV polymerase, which mediates viral genome replication and mRNA transcription, is a promising drug target. We determined the cryoelectron microscopy (cryo-EM) structure of the NiV polymerase complex, comprising the large protein (L) and phosphoprotein (P), and performed structural, biophysical, and in-depth functional analyses of the NiV polymerase. The L protein assembles with a long P tetrameric coiled-coil that is capped by a bundle of ⍺-helices that we show are likely dynamic in solution. Docking studies with a known L inhibitor clarify mechanisms of antiviral drug resistance. In addition, we identified L protein features that are required for both transcription and RNA replication and mutations that have a greater impact on RNA replication than on transcription. Our findings have the potential to aid in the rational development of drugs to combat NiV infection.
External linksCell / PubMed:39837328 / PubMed Central
MethodsEM (single particle)
Resolution2.26 Å
Structure data

44465

9bdq

EMDB-44465, PDB-9bdq:
The structure of NiV L-P complex
Method: EM (single particle) / Resolution: 2.26 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • henipavirus nipahense
KeywordsVIRAL PROTEIN / RdRp complex / L-P complex / Nipah virus

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