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TitleStructure of the Ebola virus glycoprotein spike within the virion envelope at 11 Å resolution.
Journal, issue, pagesSci Rep, Vol. 7, Page 46374, Year 2017
Publish dateApr 11, 2017
AuthorsDaniel R Beniac / Timothy F Booth /
PubMed AbstractWe present the structure of the surface Ebola virus (EBOV) trimeric glycoprotein (GP) spike at 11 Å resolution, in situ within the viral plasma membrane of purified virus particles. GP functions ...We present the structure of the surface Ebola virus (EBOV) trimeric glycoprotein (GP) spike at 11 Å resolution, in situ within the viral plasma membrane of purified virus particles. GP functions in cellular attachment, endosomal entry, and membrane fusion to initiate infection, and is a key therapeutic target. Nevertheless, only about half of the GP molecule has yet been solved to atomic resolution, excluding the mucin-like and transmembrane domains, and some of the glycans. Fitting of the atomic resolution X-ray data from expressed, truncated deletion constructs within our 11 Å structure of the entire molecule demonstrates the relationship between the GP1-GP2 domains, the mucin-like and transmembrane domains, and the bilaminar lipid envelope. We show that the mucin-like domain covers the glycan cap and partially occludes the receptor binding sites prior to proteolytic cleavage. Our structure is also consistent with key antibody neutralisation sites on GP being accessible prior to proteolysis. Based on the findings of us and others, GP-mediated binding may create an angle of 18 degrees between the planes of viral and endosomal membranes.
External linksSci Rep / PubMed:28397863 / PubMed Central
MethodsEM (single particle)
Resolution11.0 Å
Structure data

EMDB-8630:
Ebola GP spike in situ in viral membrane
Method: EM (single particle) / Resolution: 11.0 Å

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