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bioRxiv · 10.64898/2026.07.16.738223

Cryo-electron tomography of Nipah virus structural protein complexes in virus-like particles

Upadhye, V. V.·Lee, J. F.·Ercanli, N.·Ricana, C.·Hinsley, A. C.·Obr, M.·Autin, L.·Schur, F. K. M.·Aguilar, H. C.·Dick, R. A.
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Abstract

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 7[A] 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 Fs 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.

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Upadhye, V. V., Lee, J. F., Ercanli, N., Ricana, C., Hinsley, A. C., Obr, M., Autin, L., Schur, F. K. M., Aguilar, H. C., Dick, R. A.. 2026-07-17. Cryo-electron tomography of Nipah virus structural protein complexes in virus-like particles. https://doi.org/10.64898/2026.07.16.738223

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