8RYT

Structural characterization of Thogoto Virus nucleoprotein provides insights into RNA encapsidation and assembly

This is a non-PDB format compatible entry.

Summary for 8RYT

• Entry DOI: 10.2210/pdb8ryt/pdb
• EMDB information: 19599
• Descriptor: Nucleoprotein (1 entity in total)
• Functional Keywords: viral replication, nucleoprotein, rna binding, oligomerization, orthomyxovirus, viral protein
• Biological source: Thogotovirus
• Total number of polymer chains: 16
• Total formula weight: 814133.18

Authors

Roske, Y.,Mikirtumov, V.,Daumke, O.,Kudryashev, M.,Dick, A. (deposition date: 2024-02-09, release date: 2024-06-19, Last modification date: 2024-08-21)

Primary citation

Dick, A.,Mikirtumov, V.,Fuchs, J.,Krupp, F.,Olal, D.,Bendl, E.,Sprink, T.,Diebolder, C.,Kudryashev, M.,Kochs, G.,Roske, Y.,Daumke, O.
Structural characterization of Thogoto Virus nucleoprotein provides insights into viral RNA encapsidation and RNP assembly.
Structure, 32:1068-1078.e5, 2024

PubMed Abstract: Orthomyxoviruses, such as influenza and thogotoviruses, are important human and animal pathogens. Their segmented viral RNA genomes are wrapped by viral nucleoproteins (NPs) into helical ribonucleoprotein complexes (RNPs). NP structures of several influenza viruses have been reported. However, there are still contradictory models of how orthomyxovirus RNPs are assembled. Here, we characterize the crystal structure of Thogoto virus (THOV) NP and found striking similarities to structures of influenza viral NPs, including a two-lobed domain architecture, a positively charged RNA-binding cleft, and a tail loop important for trimerization and viral transcription. A low-resolution cryo-electron tomography reconstruction of THOV RNPs elucidates a left-handed double helical assembly. By providing a model for RNP assembly of THOV, our study suggests conserved NP assembly and RNA encapsidation modes for thogoto- and influenza viruses.

PubMed: 38749445
DOI: 10.1016/j.str.2024.04.016

Experimental method

ELECTRON MICROSCOPY (18 Å)