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  Ebola and Marburg virus matrix layers are locally ordered assemblies of VP40 dimers

Wan, W., Clarke, M., Norris, M. J., Kolesnikova, L., Koehler, A., Bornholdt, Z. A., et al. (2020). Ebola and Marburg virus matrix layers are locally ordered assemblies of VP40 dimers. eLife, 9: e59225. doi:10.7554/eLife.59225.

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Genre: Journal Article

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elife-59225-v3.pdf (Publisher version), 7MB
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© 2020, Wan et al.

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 Creators:
Wan, William1, Author              
Clarke, Mairi2, Author
Norris, Michael J.2, Author
Kolesnikova, Larissa2, Author
Koehler, Alexander2, Author
Bornholdt, Zachary A.2, Author
Becker, Stephan2, Author
Saphire, Erica Ollmann2, Author
Briggs, John A. G.2, Author
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

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Free keywords: CRYSTAL-STRUCTURE; PROTEIN VP40; OLIGOMERIZATION; VISUALIZATION; RESOLUTION; NUCLEOPROTEIN; PARTICLES; TOOLBOX; REVEALS; SYSTEMLife Sciences & Biomedicine - Other Topics;
 Abstract: Filoviruses such as Ebola and Marburg virus bud from the host membrane as enveloped virions. This process is achieved by the matrix protein VP40. When expressed alone, VP40 induces budding of filamentous virus-like particles, suggesting that localization to the plasma membrane, oligomerization into a matrix layer, and generation of membrane curvature are intrinsic properties of VP40. There has been no direct information on the structure of VP40 matrix layers within viruses or virus-like particles. We present structures of Ebola and Marburg VP40 matrix layers in intact virus-like particles, and within intact Marburg viruses. VP40 dimers assemble extended chains via C-terminal domain interactions. These chains stack to form 2D matrix lattices below the membrane surface. These lattices form a patchwork assembly across the membrane and suggesting that assembly may begin at multiple points. Our observations define the structure and arrangement of the matrix protein layer that mediates formation of filovirus particles.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 22
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000586608800001
DOI: 10.7554/eLife.59225
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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 9 Sequence Number: e59225 Start / End Page: - Identifier: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X