Structural highlights
Function
[VP40_EBOG4] 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 (By similarity).
Publication Abstract from PubMed
Ebola virus maturation occurs at the plasma membrane of infected cells and involves the clustering of the viral matrix protein VP40 at the assembly site as well as its interaction with the lipid bilayer. Here we report the X-ray crystal structure of VP40 from Ebola virus at 2.0 A resolution. The crystal structure reveals that Ebola virus VP40 is topologically distinct from all other known viral matrix proteins, consisting of two domains with unique folds, connected by a flexible linker. The C-terminal domain, which is absolutely required for membrane binding, contains large hydrophobic patches that may be involved in the interaction with lipid bilayers. Likewise, a highly basic region is shared between the two domains. The crystal structure reveals how the molecule may be able to switch from a monomeric conformation to a hexameric form, as observed in vitro. Its implications for the assembly process are discussed.
Crystal structure of the matrix protein VP40 from Ebola virus.,Dessen A, Volchkov V, Dolnik O, Klenk HD, Weissenhorn W EMBO J. 2000 Aug 15;19(16):4228-36. PMID:10944105[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dessen A, Volchkov V, Dolnik O, Klenk HD, Weissenhorn W. Crystal structure of the matrix protein VP40 from Ebola virus. EMBO J. 2000 Aug 15;19(16):4228-36. PMID:10944105 doi:10.1093/emboj/19.16.4228
