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TitleCryo-electron tomography of Nipah virus structural protein complexes in virus-like particles.
Journal, issue, pagesbioRxiv, Year 2026
Publish dateJul 17, 2026
AuthorsViraj V Upadhye / Jean F Lee / Nihan Ercanli / Clifton Ricana / Amy C Hinsley / Martin Obr / Ludovic Autin / Florian K M Schur / Hector C Aguilar / Robert A Dick /
PubMed AbstractNipah virus (NiV) is a BSL-4 zoonotic paramyxovirus with ~75% human mortality. The matrix protein (M) of NiV and other paramyxoviruses binds the inner leaflet of the cellular plasma membrane, ...Nipah virus (NiV) is a BSL-4 zoonotic paramyxovirus with ~75% human mortality. The matrix protein (M) of NiV and other paramyxoviruses binds the inner leaflet of the cellular plasma membrane, orchestrating virion assembly by bringing together transmembrane glycoproteins (F/G) and ribonucleoprotein complexes (N). However, the interactions of these full-length proteins within membrane complexes remain elusive. Using cryo-electron tomography and subtomogram averaging of virus like particles (VLPs), we interrogated the protein:protein interactions of the main NiV structural proteins M/N/F/G. The M lattice structure determined to 7Å revealed a novel M-dimer arrangement that yielded two distinct repeating holes. Notably, F-trimers were arranged above only one of the two holes, dependent on F's cytoplasmic tail. G was enriched in regions of higher M-VLP curvature, while N dramatically increased M-VLP pleomorphism. This work provides novel insights into paramyxoviral protein complexes, structures, and morphology.
External linksbioRxiv / PubMed:42523209 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution7.0 Å
Structure data

49696

9nqy

EMDB-49696: Subtomogram Average of the Nipah Virus Matrix Lattice in Complex with Human Cell Membrane inside Virus-Like-Particles
PDB-9nqy: Nipah Virus Matrix Lattice in Complex with Human Cell Membrane
Method: EM (subtomogram averaging) / Resolution: 7.0 Å

Source
  • henipavirus nipahense
KeywordsVIRUS LIKE PARTICLE / Assembly Lattice

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