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TitleAnalysis of a Therapeutic Antibody Cocktail Reveals Determinants for Cooperative and Broad Ebolavirus Neutralization.
Journal, issue, pagesImmunity, Vol. 52, Issue 2, Page 388-403.e12, Year 2020
Publish dateFeb 18, 2020
AuthorsPavlo Gilchuk / Charles D Murin / Jacob C Milligan / Robert W Cross / Chad E Mire / Philipp A Ilinykh / Kai Huang / Natalia Kuzmina / Pilar X Altman / Sean Hui / Bronwyn M Gunn / Aubrey L Bryan / Edgar Davidson / Benjamin J Doranz / Hannah L Turner / Tanwee Alkutkar / Robin Flinko / Chiara Orlandi / Robert Carnahan / Rachel Nargi / Robin G Bombardi / Megan E Vodzak / Sheng Li / Adaora Okoli / Morris Ibeawuchi / Benjamin Ohiaeri / George K Lewis / Galit Alter / Alexander Bukreyev / Erica Ollmann Saphire / Thomas W Geisbert / Andrew B Ward / James E Crowe /
PubMed AbstractStructural principles underlying the composition of protective antiviral monoclonal antibody (mAb) cocktails are poorly defined. Here, we exploited antibody cooperativity to develop a therapeutic mAb ...Structural principles underlying the composition of protective antiviral monoclonal antibody (mAb) cocktails are poorly defined. Here, we exploited antibody cooperativity to develop a therapeutic mAb cocktail against Ebola virus. We systematically analyzed the antibody repertoire in human survivors and identified a pair of potently neutralizing mAbs that cooperatively bound to the ebolavirus glycoprotein (GP). High-resolution structures revealed that in a two-antibody cocktail, molecular mimicry was a major feature of mAb-GP interactions. Broadly neutralizing mAb rEBOV-520 targeted a conserved epitope on the GP base region. mAb rEBOV-548 bound to a glycan cap epitope, possessed neutralizing and Fc-mediated effector function activities, and potentiated neutralization by rEBOV-520. Remodeling of the glycan cap structures by the cocktail enabled enhanced GP binding and virus neutralization. The cocktail demonstrated resistance to virus escape and protected non-human primates (NHPs) against Ebola virus disease. These data illuminate structural principles of antibody cooperativity with implications for development of antiviral immunotherapeutics.
External linksImmunity / PubMed:32023489 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.462 - 17.5 Å
Structure data

EMDB-20293:
EBOV GPdTM (Mayinga) in complex with rEBOV-548 Fab
Method: EM (single particle) / Resolution: 17.5 Å

20301

6pci

EMDB-20301, PDB-6pci:
EBOV GPdMuc (Makona) in complex with rEBOV-520 and rEBOV-548 Fabs
Method: EM (single particle) / Resolution: 4.12 Å

20947

6uye

EMDB-20947, PDB-6uye:
EBOV GPdMuc Makona bound to rEBOV-548 Fab
Method: EM (single particle) / Resolution: 3.96 Å

PDB-6oz9:
Ebola virus glycoprotein in complex with EBOV-520 Fab
Method: X-RAY DIFFRACTION / Resolution: 3.462 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • ebola virus
  • homo sapiens (human)
  • zaire ebolavirus
KeywordsVIRAL PROTEIN/Immune system / Glycoprotein / antibody / Fab / VIRAL PROTEIN / VIRAL PROTEIN-Immune system complex / immune system / Ebola / filovirus / synergy / cross-reactive / therapeutic

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