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

Moritz Hacke, Patrik Björkholm, Andrea Hellwig, Patricia Himmels, Carmen Ruiz de Almodóvar, Britta Brügger, Felix Wieland and Andreas M. Ernst ()
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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)

Nature Communications, 2015, vol. 6, issue 1, 1-9

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms8688

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