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Structure of the dengue virus envelope protein after membrane fusion

Author

Listed:
  • Yorgo Modis

    (Howard Hughes Medical Institute, Children's Hospital and Harvard Medical School)

  • Steven Ogata

    (Hawaii Biotech, Inc.)

  • David Clements

    (Hawaii Biotech, Inc.)

  • Stephen C. Harrison

    (Howard Hughes Medical Institute, Children's Hospital and Harvard Medical School)

Abstract

Dengue virus enters a host cell when the viral envelope glycoprotein, E, binds to a receptor and responds by conformational rearrangement to the reduced pH of an endosome. The conformational change induces fusion of viral and host-cell membranes. A three-dimensional structure of the soluble E ectodomain (sE) in its trimeric, postfusion state reveals striking differences from the dimeric, prefusion form. The elongated trimer bears three ‘fusion loops’ at one end, to insert into the host-cell membrane. Their structure allows us to model directly how these fusion loops interact with a lipid bilayer. The protein folds back on itself, directing its carboxy terminus towards the fusion loops. We propose a fusion mechanism driven by essentially irreversible conformational changes in E and facilitated by fusion-loop insertion into the outer bilayer leaflet. Specific features of the folded-back structure suggest strategies for inhibiting flavivirus entry.

Suggested Citation

  • Yorgo Modis & Steven Ogata & David Clements & Stephen C. Harrison, 2004. "Structure of the dengue virus envelope protein after membrane fusion," Nature, Nature, vol. 427(6972), pages 313-319, January.
    • Handle: RePEc:nat:nature:v:427:y:2004:i:6972:d:10.1038_nature02165
    DOI: 10.1038/nature02165
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    Cited by:

    1. David Moi & Shunsuke Nishio & Xiaohui Li & Clari Valansi & Mauricio Langleib & Nicolas G. Brukman & Kateryna Flyak & Christophe Dessimoz & Daniele de Sanctis & Kathryn Tunyasuvunakool & John Jumper & , 2022. "Discovery of archaeal fusexins homologous to eukaryotic HAP2/GCS1 gamete fusion proteins," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Jinliang Guo & Shangrong Li & Lisha Bai & Huimin Zhao & Wenyu Shang & Zhaojun Zhong & Tuerxunjiang Maimaiti & Xueyan Gao & Ning Ji & Yanjie Chao & Zhaofei Li & Dijun Du, 2024. "Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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