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From Proteopedia
Crystal structure demonstrating CTD-CTD interactions of Zaire Ebola virus VP40 dimer
Structural highlights
FunctionVP40_EBOZM Promotes virus assembly and budding by interacting with host proteins of the multivesicular body pathway. May facilitate virus budding by interacting with the nucleocapsid and the plasma membrane. Specific interactions with membrane-associated GP and VP24 during the budding process may also occur. The hexamer form seems to be involved in budding. The octamer form binds RNA, and may play a role in genome replication.[1] [2] Publication Abstract from PubMedFiloviruses 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. Ebola and Marburg virus matrix layers are locally ordered assemblies of VP40 dimers.,Wan W, Clarke M, Norris MJ, Kolesnikova L, Koehler A, Bornholdt ZA, Becker S, Saphire EO, Briggs JA Elife. 2020 Oct 5;9. pii: 59225. doi: 10.7554/eLife.59225. PMID:33016878[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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