Atomic model of vesicular stomatitis virus and mechanism of assembly.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
10 10 2022
10 10 2022
Historique:
received:
04
05
2022
accepted:
27
09
2022
entrez:
10
10
2022
pubmed:
11
10
2022
medline:
13
10
2022
Statut:
epublish
Résumé
Like other negative-strand RNA viruses (NSVs) such as influenza and rabies, vesicular stomatitis virus (VSV) has a three-layered organization: a layer of matrix protein (M) resides between the glycoprotein (G)-studded membrane envelope and the nucleocapsid, which is composed of the nucleocapsid protein (N) and the encapsidated genomic RNA. Lack of in situ atomic structures of these viral components has limited mechanistic understanding of assembling the bullet-shaped virion. Here, by cryoEM and sub-particle reconstruction, we have determined the in situ structures of M and N inside VSV at 3.47 Å resolution. In the virion, N and M sites have a stoichiometry of 1:2. The in situ structures of both N and M differ from their crystal structures in their N-terminal segments and oligomerization loops. N-RNA, N-N, and N-M-M interactions govern the formation of the capsid. A double layer of M contributes to packaging of the helical nucleocapsid: the inner M (IM) joins neighboring turns of the N helix, while the outer M (OM) contacts G and the membrane envelope. The pseudo-crystalline organization of G is further mapped by cryoET. The mechanism of VSV assembly is delineated by the network interactions of these viral components.
Identifiants
pubmed: 36216930
doi: 10.1038/s41467-022-33664-4
pii: 10.1038/s41467-022-33664-4
pmc: PMC9549855
doi:
Substances chimiques
Glycoproteins
0
Nucleocapsid Proteins
0
RNA, Viral
0
RNA
63231-63-0
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
5980Subventions
Organisme : NIAID NIH HHS
ID : R01 AI094386
Pays : United States
Organisme : NIH HHS
ID : S10 OD018111
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI171426
Pays : United States
Organisme : NIGMS NIH HHS
ID : U24 GM116792
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM071940
Pays : United States
Informations de copyright
© 2022. The Author(s).
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