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| Title | Structural Characterization of Pan-Ebolavirus Antibody 6D6 Targeting the Fusion Peptide of the Surface Glycoprotein. |
|---|---|
| Journal, issue, pages | J Infect Dis, Vol. 219, Issue 3, Page 415-419, Year 2019 |
| Publish date | Jan 9, 2019 |
 Authors | Jacob C Milligan / Diptiben V Parekh / Katherine M Fuller / Manabu Igarashi / Ayato Takada / Erica Ollmann Saphire /   |
| PubMed Abstract | Ebola virus infection causes severe disease in humans and represents a global health threat. Candidates for immunotherapeutics and vaccines have shown promise in clinical trials, although they are ...Ebola virus infection causes severe disease in humans and represents a global health threat. Candidates for immunotherapeutics and vaccines have shown promise in clinical trials, although they are ineffective against other members of the Ebolavirus genus that also cause periodic, lethal outbreaks. In this study, we present a crystal structure of a pan-ebolavirus antibody, 6D6, as well as single-particle electron microscopy reconstructions of 6D6 in complex with Ebola and Bundibugyo virus glycoproteins. 6D6 binds to the conserved glycoprotein fusion peptide, implicating it as a site of immune vulnerability that could be exploited to reliably elicit a pan-ebolavirus neutralizing antibody response. |
 External links | J Infect Dis / PubMed:30203042 / PubMed Central |
| Methods | EM (single particle) / X-ray diffraction |
| Resolution | 1.96 - 20.0 Å |
| Structure data |  EMDB-9048:  EMDB-9049:  PDB-6dg2: |
| Chemicals |  ChemComp-HOH: |
| Source |
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 Keywords |  IMMUNE SYSTEM / Antibody / Monoclonal / Antigen Binding Fragment / Fab / Ebola |
