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TitleAsymmetric and non-stoichiometric glycoprotein recognition by two distinct antibodies results in broad protection against ebolaviruses.
Journal, issue, pagesCell, Vol. 185, Issue 6, Page 995-1007.e18, Year 2022
Publish dateMar 17, 2022
AuthorsJacob C Milligan / Carl W Davis / Xiaoying Yu / Philipp A Ilinykh / Kai Huang / Peter J Halfmann / Robert W Cross / Viktoriya Borisevich / Krystle N Agans / Joan B Geisbert / Chakravarthy Chennareddy / Arthur J Goff / Ashley E Piper / Sean Hui / Kelly C L Shaffer / Tierra Buck / Megan L Heinrich / Luis M Branco / Ian Crozier / Michael R Holbrook / Jens H Kuhn / Yoshihiro Kawaoka / Pamela J Glass / Alexander Bukreyev / Thomas W Geisbert / Gabriella Worwa / Rafi Ahmed / Erica Ollmann Saphire /
PubMed AbstractSeveral ebolaviruses cause outbreaks of severe disease. Vaccines and monoclonal antibody cocktails are available to treat Ebola virus (EBOV) infections, but not Sudan virus (SUDV) or other ...Several ebolaviruses cause outbreaks of severe disease. Vaccines and monoclonal antibody cocktails are available to treat Ebola virus (EBOV) infections, but not Sudan virus (SUDV) or other ebolaviruses. Current cocktails contain antibodies that cross-react with the secreted soluble glycoprotein (sGP) that absorbs virus-neutralizing antibodies. By sorting memory B cells from EBOV infection survivors, we isolated two broadly reactive anti-GP monoclonal antibodies, 1C3 and 1C11, that potently neutralize, protect rodents from disease, and lack sGP cross-reactivity. Both antibodies recognize quaternary epitopes in trimeric ebolavirus GP. 1C11 bridges adjacent protomers via the fusion loop. 1C3 has a tripartite epitope in the center of the trimer apex. One 1C3 antigen-binding fragment anchors simultaneously to the three receptor-binding sites in the GP trimer, and separate 1C3 paratope regions interact differently with identical residues on the three protomers. A cocktail of both antibodies completely protected nonhuman primates from EBOV and SUDV infections, indicating their potential clinical value.
External linksCell / PubMed:35303429 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.15 - 3.59 Å
Structure data

25471

7swd

EMDB-25471, PDB-7swd:
Structure of EBOV GP lacking the mucin-like domain with 1C11 scFv and 1C3 Fab bound
Method: EM (single particle) / Resolution: 3.59 Å

PDB-7n6p:
Crystal structure of the anti-EBOV and SUDV monoclonal antibody 1C3 Fab
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • ebola virus - gabon (1994-1997)
  • zaire ebolavirus
KeywordsIMMUNE SYSTEM / glycoprotein / antibody / VIRAL PROTEIN/Immune System / VIRAL PROTEIN / Ebola virus / VIRAL PROTEIN-Immune System complex

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