Issue Date: July 14, 2008
Structure of Ebola Virus Surface Glycoprotein
After a five-year effort, researchers have determined the structure of the Ebola virus surface glycoprotein, which enables the virus to enter cells. They analyzed the glycoprotein bound to an antibody from a rare survivor of a 1995 Ebola outbreak in Congo (Nature 2008, 454, 177). The work aids in understanding the mechanism by which Ebola virus enters cells and could help lead to immunotherapeutics. Ebola virus kills more than half of those infected by causing hemorrhagic fever—dehydration, bleeding, and shock. There's no effective treatment. The new structure, obtained by Erica Ollmann Saphire, Jeffrey E. Lee, Dennis R. Burton, and coworkers at Scripps Research Institute in La Jolla, Calif., shows how the survivor's antibody (yellow) bridges the trimeric glycoprotein's GP1 host-attachment subunits (light blue, dark blue, and teal) and GP2 membrane fusion-inducing subunits (white). It reveals how the subunits might mediate cell attachment and membrane fusion while masking themselves from immune surveillance. The new structural data also help explain why anti-Ebola antibodies are so rare, identify the few surface sites to which antibodies might bind, and provide a template for vaccine and antibody design, Ollmann Saphire notes.
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