7UML

Structure of vesicular stomatitis virus (local reconstruction, 3.5 A resolution)

Summary for 7UML

• Entry DOI: 10.2210/pdb7uml/pdb
• EMDB information: 26602 26603
• Descriptor: Nucleoprotein, Matrix protein, RNA (5'-R(P*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3') (3 entities in total)
• Functional Keywords: vesicular stomatitis virus, bullet-shaped particle, rhrabdovirus, nucleocapsid, helical reconstruction, cryo electron microscopy, nucleoprotein, matrix protein, rna, assembly, viral protein-rna complex, viral protein/rna
• Biological source: Vesicular stomatitis Indiana virus; More
• Total number of polymer chains: 7
• Total formula weight: 224636.21

Authors

Jenni, S.,Horwitz, J.A.,Bloyet, L.-M.,Whelan, S.P.J.,Harrison, S.C. (deposition date: 2022-04-07, release date: 2022-04-20, Last modification date: 2024-02-14)

Primary citation

Jenni, S.,Horwitz, J.A.,Bloyet, L.M.,Whelan, S.P.J.,Harrison, S.C.
Visualizing molecular interactions that determine assembly of a bullet-shaped vesicular stomatitis virus particle.
Nat Commun, 13:4802-4802, 2022

PubMed Abstract: Vesicular stomatitis virus (VSV) is a negative-strand RNA virus with a non-segmented genome, closely related to rabies virus. Both have characteristic bullet-like shapes. We report the structure of intact, infectious VSV particles determined by cryogenic electron microscopy. By compensating for polymorphism among viral particles with computational classification, we obtained a reconstruction of the shaft ("trunk") at 3.5 Å resolution, with lower resolution for the rounded tip. The ribonucleoprotein (RNP), genomic RNA complexed with nucleoprotein (N), curls into a dome-like structure with about eight gradually expanding turns before transitioning into the regular helical trunk. Two layers of matrix (M) protein link the RNP with the membrane. Radial inter-layer subunit contacts are fixed within single RNA-N-M1-M2 modules, but flexible lateral and axial interactions allow assembly of polymorphic virions. Together with published structures of recombinant N in various states, our results suggest a mechanism for membrane-coupled self-assembly of VSV and its relatives.

PubMed: 35970826
DOI: 10.1038/s41467-022-32223-1

Experimental method

ELECTRON MICROSCOPY (3.5 Å)