A conserved glutathione binding site in poliovirus is a target for antivirals and vaccine stabilisation

Mohammad W. Bahar; Veronica Nasta; Helen Fox; Lee Sherry; Keith Grehan; Claudine Porta; Andrew J. Macadam; Nicola J. Stonehouse; David J. Rowlands; Elizabeth E. Fry; David I. Stuart

doi:10.1038/s42003-022-04252-5

Communications Biology (Nov 2022)

A conserved glutathione binding site in poliovirus is a target for antivirals and vaccine stabilisation

Mohammad W. Bahar,
Veronica Nasta,
Helen Fox,
Lee Sherry,
Keith Grehan,
Claudine Porta,
Andrew J. Macadam,
Nicola J. Stonehouse,
David J. Rowlands,
Elizabeth E. Fry,
David I. Stuart

Affiliations

Mohammad W. Bahar: Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington
Veronica Nasta: Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington
Helen Fox: The National Institute for Biological Standards and Control
Lee Sherry: Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds
Keith Grehan: Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds
Claudine Porta: Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington
Andrew J. Macadam: The National Institute for Biological Standards and Control
Nicola J. Stonehouse: Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds
David J. Rowlands: Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds
Elizabeth E. Fry: Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington
David I. Stuart: Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington

DOI: https://doi.org/10.1038/s42003-022-04252-5
Journal volume & issue: Vol. 5, no. 1
pp. 1 – 12

Abstract

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Cryo-EM structures reveal the role of glutathione (GSH) in poliovirus (PV) serotype 3 virus-like particle (VLP) stability, suggesting GSH or an analogous tight-binding antiviral offers potential for stabilizing VLP vaccines against PV.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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