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TitleCryo-EM structures of Nipah virus polymerase complex reveal highly varied interactions between L and P proteins among paramyxoviruses.
Journal, issue, pagesProtein Cell, Vol. 16, Issue 8, Page 705-723, Year 2025
Publish dateAug 7, 2025
AuthorsLu Xue / Tiancai Chang / Jiacheng Gui / Zimu Li / Heyu Zhao / Binqian Zou / Junnan Lu / Mei Li / Xin Wen / Shenghua Gao / Peng Zhan / Lijun Rong / Liqiang Feng / Peng Gong / Jun He / Xinwen Chen / Xiaoli Xiong /
PubMed AbstractNipah virus (NiV) and related viruses form a distinct henipavirus genus within the Paramyxoviridae family. NiV continues to spillover into the humans causing deadly outbreaks with increasing human- ...Nipah virus (NiV) and related viruses form a distinct henipavirus genus within the Paramyxoviridae family. NiV continues to spillover into the humans causing deadly outbreaks with increasing human-bat interaction. NiV encodes the large protein (L) and phosphoprotein (P) to form the viral RNA polymerase machinery. Their sequences show limited homologies to those of non-henipavirus paramyxoviruses. We report two cryo-electron microscopy (cryo-EM) structures of the Nipah virus (NiV) polymerase L-P complex, expressed and purified in either its full-length or truncated form. The structures resolve the RNA-dependent RNA polymerase (RdRp) and polyribonucleotidyl transferase (PRNTase) domains of the L protein, as well as a tetrameric P protein bundle bound to the L-RdRp domain. L-protein C-terminal regions are unresolved, indicating flexibility. Two PRNTase domain zinc-binding sites, conserved in most Mononegavirales, are confirmed essential for NiV polymerase activity. The structures further reveal anchoring of the P protein bundle and P protein X domain (XD) linkers on L, via an interaction pattern distinct among Paramyxoviridae. These interactions facilitate binding of a P protein XD linker in the nucleotide entry channel and distinct positioning of other XD linkers. We show that the disruption of the L-P interactions reduces NiV polymerase activity. The reported structures should facilitate rational antiviral-drug discovery and provide a guide for the functional study of NiV polymerase.
External linksProtein Cell / PubMed:39964914 / PubMed Central
MethodsEM (single particle)
Resolution2.31 - 2.52 Å
Structure data

60922

9iv9

EMDB-60922, PDB-9iv9:
Cryo-EM structure of a truncated Nipah Virus L Protein bound by Phosphoprotein Tetramer
Method: EM (single particle) / Resolution: 2.31 Å

60923

9iva

EMDB-60923, PDB-9iva:
Cryo-EM structure of the full-length Nipah Virus L Protein bound by Phosphoprotein Tetramer
Method: EM (single particle) / Resolution: 2.52 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • henipavirus nipahense
KeywordsVIRAL PROTEIN / RNA polymerase

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