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TitleStructures of Ebola virus GP and sGP in complex with therapeutic antibodies.
Journal, issue, pagesNat Microbiol, Vol. 1, Issue 9, Page 16128, Year 2016
Publish dateAug 8, 2016
AuthorsJesper Pallesen / Charles D Murin / Natalia de Val / Christopher A Cottrell / Kathryn M Hastie / Hannah L Turner / Marnie L Fusco / Andrew I Flyak / Larry Zeitlin / James E Crowe / Kristian G Andersen / Erica Ollmann Saphire / Andrew B Ward /
PubMed AbstractThe Ebola virus (EBOV) GP gene encodes two glycoproteins. The major product is a soluble, dimeric glycoprotein (sGP) that is secreted abundantly. Despite the abundance of sGP during infection, little ...The Ebola virus (EBOV) GP gene encodes two glycoproteins. The major product is a soluble, dimeric glycoprotein (sGP) that is secreted abundantly. Despite the abundance of sGP during infection, little is known regarding its structure or functional role. A minor product, resulting from transcriptional editing, is the transmembrane-anchored, trimeric viral surface glycoprotein (GP). GP mediates attachment to and entry into host cells, and is the intended target of antibody therapeutics. Because large portions of sequence are shared between GP and sGP, it has been hypothesized that sGP may potentially subvert the immune response or may contribute to pathogenicity. In this study, we present cryo-electron microscopy structures of GP and sGP in complex with GP-specific and GP/sGP cross-reactive antibodies undergoing human clinical trials. The structure of the sGP dimer presented here, in complex with both an sGP-specific antibody and a GP/sGP cross-reactive antibody, permits us to unambiguously assign the oligomeric arrangement of sGP and compare its structure and epitope presentation to those of GP. We also provide biophysical evaluation of naturally occurring GP/sGP mutations that fall within the footprints identified by our high-resolution structures. Taken together, our data provide a detailed and more complete picture of the accessible Ebolavirus glycoprotein landscape and a structural basis to evaluate patient and vaccine antibody responses towards differently structured products of the GP gene.
External linksNat Microbiol / PubMed:27562261 / PubMed Central
MethodsEM (single particle)
Resolution4.3 - 5.5 Å
Structure data

8240

5kel

EMDB-8240: EBOV GP in complex with IgG c2G4 and c13C6 Fabs
PDB-5kel: EBOV GP in complex with variable Fab domains of IgGs c2G4 and c13C6
Method: EM (single particle) / Resolution: 4.3 Å

8241

5kem

EMDB-8241: EBOV sGP in complex with IgG c13C6 and BDBV91 Fabs
PDB-5kem: EBOV sGP in complex with variable Fab domains of IgGs c13C6 and BDBV91
Method: EM (single particle) / Resolution: 5.5 Å

8242

5ken

EMDB-8242: EBOV GP in complex with IgG c4G7 and c13C6 Fabs
PDB-5ken: EBOV GP in complex with variable Fab domains of IgGs c4G7 and c13C6
Method: EM (single particle) / Resolution: 4.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • zaire ebolavirus
  • zaire ebolavirus (strain mayinga-76)
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / Ebola virus surface glycoprotein / therapeutic antibody cocktail / ZMapp / VIRAL PROTEIN-IMMUNE SYSTEM complex / Ebola virus secreted glycoprotein / sGP / antibodies

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