Structural highlights
Publication Abstract from PubMed
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, though they are ineffective against other members of the Ebolavirus genus which also cause periodic, lethal outbreaks. Here, 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.
Structural Characterization of Pan-ebolavirus Antibody 6D6 Targeting the Fusion Peptide of the Surface Glycoprotein.,Milligan JC, Parekh DV, Fuller KM, Igarashi M, Takada A, Saphire EO J Infect Dis. 2018 Sep 10. pii: 5093891. doi: 10.1093/infdis/jiy532. PMID:30203042[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Milligan JC, Parekh DV, Fuller KM, Igarashi M, Takada A, Saphire EO. Structural Characterization of Pan-ebolavirus Antibody 6D6 Targeting the Fusion Peptide of the Surface Glycoprotein. J Infect Dis. 2018 Sep 10. pii: 5093891. doi: 10.1093/infdis/jiy532. PMID:30203042 doi:http://dx.doi.org/10.1093/infdis/jiy532