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Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor

Author

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  • Jeffrey E. Lee

    (The Scripps Research Institute, 10550 North Torrey Pines Road, Mail Drop IMM-2, La Jolla, California 92037, USA)

  • Marnie L. Fusco

    (The Scripps Research Institute, 10550 North Torrey Pines Road, Mail Drop IMM-2, La Jolla, California 92037, USA)

  • Ann J. Hessell

    (The Scripps Research Institute, 10550 North Torrey Pines Road, Mail Drop IMM-2, La Jolla, California 92037, USA)

  • Wendelien B. Oswald

    (The Scripps Research Institute, 10550 North Torrey Pines Road, Mail Drop IMM-2, La Jolla, California 92037, USA)

  • Dennis R. Burton

    (The Scripps Research Institute, 10550 North Torrey Pines Road, Mail Drop IMM-2, La Jolla, California 92037, USA)

  • Erica Ollmann Saphire

    (The Scripps Research Institute, 10550 North Torrey Pines Road, Mail Drop IMM-2, La Jolla, California 92037, USA)

Abstract

Ebola virus (EBOV) entry requires the surface glycoprotein (GP) to initiate attachment and fusion of viral and host membranes. Here we report the crystal structure of EBOV GP in its trimeric, pre-fusion conformation (GP1+GP2) bound to a neutralizing antibody, KZ52, derived from a human survivor of the 1995 Kikwit outbreak. Three GP1 viral attachment subunits assemble to form a chalice, cradled by the GP2 fusion subunits, while a novel glycan cap and projected mucin-like domain restrict access to the conserved receptor-binding site sequestered in the chalice bowl. The glycocalyx surrounding GP is likely central to immune evasion and may explain why survivors have insignificant neutralizing antibody titres. KZ52 recognizes a protein epitope at the chalice base where it clamps several regions of the pre-fusion GP2 to the amino terminus of GP1. This structure provides a template for unravelling the mechanism of EBOV GP-mediated fusion and for future immunotherapeutic development.

Suggested Citation

  • Jeffrey E. Lee & Marnie L. Fusco & Ann J. Hessell & Wendelien B. Oswald & Dennis R. Burton & Erica Ollmann Saphire, 2008. "Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor," Nature, Nature, vol. 454(7201), pages 177-182, July.
    • Handle: RePEc:nat:nature:v:454:y:2008:i:7201:d:10.1038_nature07082
    DOI: 10.1038/nature07082
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    Cited by:

    1. Phillips, J.C., 2015. "Similarity is not enough: Tipping points of Ebola Zaire mortalities," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 427(C), pages 277-281.
    2. Wen-Han Yu & Peng Zhao & Monia Draghi & Claudia Arevalo & Christina B Karsten & Todd J Suscovich & Bronwyn Gunn & Hendrik Streeck & Abraham L Brass & Michael Tiemeyer & Michael Seaman & John R Mascola, 2018. "Exploiting glycan topography for computational design of Env glycoprotein antigenicity," PLOS Computational Biology, Public Library of Science, vol. 14(4), pages 1-28, April.
    3. Nicole V. Johnson & Revina C. Scherpenzeel & Mark J. G. Bakkers & Ajit R. Ramamohan & Daan Overveld & Lam Le & Johannes P. M. Langedijk & Joost A. Kolkman & Jason S. McLellan, 2024. "Structural basis for potent neutralization of human respirovirus type 3 by protective single-domain camelid antibodies," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    4. Nicholas V. Olijnyk, 2015. "An algorithmic historiography of the Ebola research specialty: mapping the science behind Ebola," Scientometrics, Springer;Akadémiai Kiadó, vol. 105(1), pages 623-643, October.

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