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Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography

Author

Listed:
  • James E. Voss

    (Institut Pasteur, Unité de Virologie Structurale, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
    CNRS URA 3015, 25 rue du Dr Roux, 75724 Paris Cedex 15, France)

  • Marie-Christine Vaney

    (Institut Pasteur, Unité de Virologie Structurale, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
    CNRS URA 3015, 25 rue du Dr Roux, 75724 Paris Cedex 15, France)

  • Stéphane Duquerroy

    (Institut Pasteur, Unité de Virologie Structurale, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
    CNRS URA 3015, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
    Université Paris-Sud, Faculté d’Orsay)

  • Clemens Vonrhein

    (Global Phasing Ltd, Sheraton House, Castle Park)

  • Christine Girard-Blanc

    (Institut Pasteur, Plateforme de Production de protéines recombinantes, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
    CNRS URA 2185, 25 rue du Dr Roux, 75724 Paris Cedex 15, France)

  • Elodie Crublet

    (Institut Pasteur, Plateforme de Production de protéines recombinantes, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
    CNRS URA 2185, 25 rue du Dr Roux, 75724 Paris Cedex 15, France)

  • Andrew Thompson

    (Synchrotron SOLEIL, L’Orme de Merisiers, BP 48 St Aubin, 91192 Gif sur Yvette, France)

  • Gérard Bricogne

    (Global Phasing Ltd, Sheraton House, Castle Park)

  • Félix A. Rey

    (Institut Pasteur, Unité de Virologie Structurale, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
    CNRS URA 3015, 25 rue du Dr Roux, 75724 Paris Cedex 15, France)

Abstract

The pH-sensitive mechanism that gets alphaviruses into host cells Alphaviruses are significant animal and human pathogens — as demonstrated in recent outbreaks of infection with the mosquito-borne Chikungunya virus in India and southeast Asia. The E1 and E2 glycoproteins of alphaviruses are central to the way the virus infects host cells. The E1/E2 heterodimers that form spikes on the virus surface dissociate in the acidic conditions found in the internal vesicles of host cells, and E1 triggers infection by fusing with the endosomal membrane. Félix Rey and colleagues present the structure of Chikungunya virus envelope glycoprotein at neutral pH, and Michael Rossmann and colleagues reveal the structure of the envelope proteins of Sindbis virus at low pH. Sindbis virus can cause fever in humans and is the most extensively studied alphavirus. Comparison of the two structures provides insight into how fusion activation is controlled and points to possible vaccine targets.

Suggested Citation

  • James E. Voss & Marie-Christine Vaney & Stéphane Duquerroy & Clemens Vonrhein & Christine Girard-Blanc & Elodie Crublet & Andrew Thompson & Gérard Bricogne & Félix A. Rey, 2010. "Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography," Nature, Nature, vol. 468(7324), pages 709-712, December.
    • Handle: RePEc:nat:nature:v:468:y:2010:i:7324:d:10.1038_nature09555
    DOI: 10.1038/nature09555
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    Citations

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    Cited by:

    1. Xiaofeng Zhai & Xiaoling Li & Michael Veit & Ningning Wang & Yu Wang & Andres Merits & Zhiwen Jiang & Yan Qin & Xiaoguang Zhang & Kaili Qi & Houqi Jiao & Wan-Ting He & Ye Chen & Yang Mao & Shuo Su, 2024. "LDLR is used as a cell entry receptor by multiple alphaviruses," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Vidya Mangala Prasad & Jelle S. Blijleven & Jolanda M. Smit & Kelly K. Lee, 2022. "Visualization of conformational changes and membrane remodeling leading to genome delivery by viral class-II fusion machinery," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Samantha Hover & Frank W. Charlton & Jan Hellert & Jessica J. Swanson & Jamel Mankouri & John N. Barr & Juan Fontana, 2023. "Organisation of the orthobunyavirus tripodal spike and the structural changes induced by low pH and K+ during entry," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    4. 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.
    5. Marie-Christine Vaney & Mariano Dellarole & Stéphane Duquerroy & Iris Medits & Georgios Tsouchnikas & Alexander Rouvinski & Patrick England & Karin Stiasny & Franz X. Heinz & Félix A. Rey, 2022. "Evolution and activation mechanism of the flavivirus class II membrane-fusion machinery," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    6. Ningning Wang & Andres Merits & Michael Veit & Laura Sandra Lello & Shuhan Kong & Houqi Jiao & Jie Chen & Yu Wang & Georgi Dobrikov & Félix A. Rey & Shuo Su, 2024. "LDL receptor in alphavirus entry: structural analysis and implications for antiviral therapy," Nature Communications, Nature, vol. 15(1), pages 1-7, December.
    7. Pan Yang & Wanyu Li & Xiaoyi Fan & Junhua Pan & Colin J. Mann & Haley Varnum & Lars E. Clark & Sarah A. Clark & Adrian Coscia & Himanish Basu & Katherine Nabel Smith & Vesna Brusic & Jonathan Abraham, 2024. "Structural basis for VLDLR recognition by eastern equine encephalitis virus," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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