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PMID: 20198110 Published · ppublish English Journal Article

Ebolavirus glycoprotein structure and mechanism of entry.

Future virology ·Vol. 4 ·No. 6 ·2009-00-00 ·Pages 621-635

Lee JE, Saphire EO

Abstract

Ebolavirus (EBOV) is a highly virulent pathogen capable of causing a severe hemorrhagic fever with 50-90% lethality. The EBOV glycoprotein (GP) is the only virally expressed protein on the virion surface and is critical for attachment to host cells and catalysis of membrane fusion. Hence, the EBOV GP is a critical component of vaccines as well as a target of neutralizing antibodies and inhibitors of attachment and fusion. The crystal structure of the Zaire ebolavirus GP in its trimeric, prefusion conformation (3 GP(1) plus 3 GP(2)) in complex with a neutralizing antibody fragment, derived from a human survivor of the 1995 Kikwit outbreak, was recently determined. This is the first near-complete structure of any filovirus glycoprotein. The overall molecular architecture of the Zaire ebolavirus GP and its role in viral entry and membrane fusion are discussed in this article.

Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lee Jeffrey E
Department of Immunology & Microbial Science, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA, Tel.: +1 858 784 7976.
Saphire Erica Ollmann
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Article Info
Journal
Future virology
Abbr.
Future Virol
ISSN
1746-0794
Published
2009-00-00
Pages
621-635
Language
English
Region
England
NLM ID
101278124
PMCID
PMC2829775
Grants
NIAID NIH HHS · R21 AI053423-01 · United States
NIAID NIH HHS · R01 AI081982 · United States
NIAID NIH HHS · R01 AI067927 · United States
NIAID NIH HHS · R01 AI081982-01A1 · United States
NIAID NIH HHS · R01 AI067927-04 · United States
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