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-Structure paper
タイトル | Atomic model of vesicular stomatitis virus and mechanism of assembly. |
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ジャーナル・号・ページ | Nat Commun, Vol. 13, Issue 1, Page 5980, Year 2022 |
掲載日 | 2022年10月10日 |
著者 | Kang Zhou / Zhu Si / Peng Ge / Jun Tsao / Ming Luo / Z Hong Zhou / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:36216930 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 3.47 Å |
構造データ | EMDB-26841, PDB-7uws: |
由来 |
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キーワード | VIRAL PROTEIN/RNA / Vesicular stomatitis virus / Nucleocapsid / Matrix protein M / Nucleocapsid protein N / VIRAL PROTEIN-RNA complex |