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Ethanol Inactivation of Enveloped Viruses: Structural and Surface Chemistry Insights into Phi6

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    Ethanol Inactivation of Enveloped Viruses: Structural and Surface Chemistry Insights into Phi6
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    • Samuel Watts
      Samuel Watts
      Department of Chemistry, University of Fribourg, Chemin du Musée 9, 1700 Fribourg, Switzerland
      Laboratory for Biointerfaces, Empa, Swiss Federal Laboratories for Material Science and Technology, Lerchenfeldstrasse 5, 9014 St. Gallen, Switzerland
      More by Samuel Watts
    • Madeleine Ramstedt
      Madeleine Ramstedt
      Department of Chemistry, Umeå University, 90187 Umeå, Sweden
      More by Madeleine Ramstedt
    • Stefan Salentinig*
      Stefan Salentinig
      Department of Chemistry, University of Fribourg, Chemin du Musée 9, 1700 Fribourg, Switzerland
      *[email protected]
      More by Stefan Salentinig
      Orcidhttps://orcid.org/0000-0002-7541-2734
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    The Journal of Physical Chemistry Letters

    Cite this: J. Phys. Chem. Lett. 2021, 12, 39, 9557–9563
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    https://doi.org/10.1021/acs.jpclett.1c02327
    Published September 28, 2021
    Copyright © 2021 American Chemical Society
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    Abstract

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    Lipid-enveloped viruses, such as Ebola, influenza, or coronaviruses, are a major threat to human health. Ethanol is an efficient disinfectant that is widely used to inactivate these viruses and prevent their transmission. However, the interactions between ethanol and enveloped viruses leading to their inactivation are not yet fully understood. This study demonstrates the link between ethanol-induced viral inactivation and the nanostructural and chemical transformations of the model virus Phi6, an 85 nm diameter lipid-enveloped bacterial virus that is commonly used as surrogate for human pathogenic viruses. The virus morphology was investigated using small-angle X-ray scattering and dynamic light scattering and was related to its infectivity. The Phi6’s surface chemistry was characterized by cryogenic X-ray photoelectron spectroscopy, and the modifications in protein structure were assessed by circular dichroism and fluorescence spectroscopy. Ethanol-triggered structural modifications were found in the lipid envelope, detaching from the protein capsid and forming coexisting nanostructures.

    Copyright © 2021 American Chemical Society

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    Supporting Information

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    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.jpclett.1c02327.

    • Supporting material and methods: buffer preparation, virus production, virus purification, ethanol treatment and biological activity, cryo-XPS, SAXS measurement, SAXS data analysis, cryo-TEM, DLS, CD spectroscopy, and fluorescence spectroscopy (PDF)

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    The Journal of Physical Chemistry Letters

    Cite this: J. Phys. Chem. Lett. 2021, 12, 39, 9557–9563
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.jpclett.1c02327
    Published September 28, 2021
    Copyright © 2021 American Chemical Society
    Request reuse permissions

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