IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v6y2015i1d10.1038_ncomms8688.html
   My bibliography  Save this article

Inhibition of Ebola virus glycoprotein-mediated cytotoxicity by targeting its transmembrane domain and cholesterol

Author

Listed:
  • Moritz Hacke

    (Heidelberg University Biochemistry Center (BZH))

  • Patrik Björkholm

    (Cell and Molecular Biology, Science for Life Laboratory, Uppsala University)

  • Andrea Hellwig

    (Interdisciplinary Center for Neurosciences, Heidelberg University)

  • Patricia Himmels

    (Heidelberg University Biochemistry Center (BZH))

  • Carmen Ruiz de Almodóvar

    (Heidelberg University Biochemistry Center (BZH))

  • Britta Brügger

    (Heidelberg University Biochemistry Center (BZH))

  • Felix Wieland

    (Heidelberg University Biochemistry Center (BZH))

  • Andreas M. Ernst

    (Heidelberg University Biochemistry Center (BZH))

Abstract

The high pathogenicity of the Ebola virus reflects multiple concurrent processes on infection. Among other important determinants, Ebola fusogenic glycoprotein (GP) has been associated with the detachment of infected cells and eventually leads to vascular leakage and haemorrhagic fever. Here we report that the membrane-anchored GP is sufficient to induce the detachment of adherent cells. The results show that the detachment induced through either full-length GP1,2 or the subunit GP2 depends on cholesterol and the structure of the transmembrane domain. These data reveal a novel molecular mechanism in which GP regulates Ebola virus assembly and suggest that cholesterol-reducing agents could be useful as therapeutics to counteract GP-mediated cell detachment.

Suggested Citation

  • Moritz Hacke & Patrik Björkholm & Andrea Hellwig & Patricia Himmels & Carmen Ruiz de Almodóvar & Britta Brügger & Felix Wieland & Andreas M. Ernst, 2015. "Inhibition of Ebola virus glycoprotein-mediated cytotoxicity by targeting its transmembrane domain and cholesterol," Nature Communications, Nature, vol. 6(1), pages 1-9, November.
  • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8688
    DOI: 10.1038/ncomms8688
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms8688
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/ncomms8688?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Jing Zhang & Bin Wang & Xiaoxiao Gao & Cheng Peng & Chao Shan & Silas F. Johnson & Richard C. Schwartz & Yong-Hui Zheng, 2022. "RNF185 regulates proteostasis in Ebolavirus infection by crosstalk between the calnexin cycle, ERAD, and reticulophagy," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Sarah Goellner & Giray Enkavi & Vibhu Prasad & Solène Denolly & Sungmin Eu & Giulia Mizzon & Leander Witte & Waldemar Kulig & Zina M. Uckeley & Teresa M. Lavacca & Uta Haselmann & Pierre-Yves Lozach &, 2023. "Zika virus prM protein contains cholesterol binding motifs required for virus entry and assembly," Nature Communications, Nature, vol. 14(1), pages 1-20, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8688. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.