2012年3月13日
Structural dissection of Ebola virus and its assembly determinants using cryo-electron tomography.
Proceedings of the National Academy of Sciences of the United States of America
- ,
- ,
- ,
- ,
- ,
- ,
- ,
- 巻
- 109
- 号
- 11
- 開始ページ
- 4275
- 終了ページ
- 80
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1073/pnas.1120453109
- 出版者・発行元
- NATL ACAD SCIENCES
Ebola virus is a highly pathogenic filovirus causing severe hemorrhagic fever with high mortality rates. It assembles heterogenous, filamentous, enveloped virus particles containing a negative-sense, single-stranded RNA genome packaged within a helical nucleocapsid (NC). We have used cryo-electron microscopy and tomography to visualize Ebola virus particles, as well as Ebola virus-like particles, in three dimensions in a near-native state. The NC within the virion forms a left-handed helix with an inner nucleoprotein layer decorated with protruding arms composed of VP24 and VP35. A comparison with the closely related Marburg virus shows that the N-terminal region of nucleoprotein defines the inner diameter of the Ebola virus NC, whereas the RNA genome defines its length. Binding of the nucleoprotein to RNA can assemble a loosely coiled NC-like structure; the loose coil can be condensed by binding of the viral matrix protein VP40 to the C terminus of the nucleoprotein, and rigidified by binding of VP24 and VP35 to alternate copies of the nucleoprotein. Four proteins (NP, VP24, VP35, and VP40) are necessary and sufficient to mediate assembly of an NC with structure, symmetry, variability, and flexibility indistinguishable from that in Ebola virus particles released from infected cells. Together these data provide a structural and architectural description of Ebola virus and define the roles of viral proteins in its structure and assembly.
- リンク情報
-
- DOI
- https://doi.org/10.1073/pnas.1120453109
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/22371572
- PubMed Central
- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3306676
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000301426700052&DestApp=WOS_CPL
- ID情報
-
- DOI : 10.1073/pnas.1120453109
- ISSN : 0027-8424
- PubMed ID : 22371572
- PubMed Central 記事ID : PMC3306676
- Web of Science ID : WOS:000301426700052