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Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities
The Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Faculty of Health and Medical Sciences, Blegdamsvej 3B, Copenhagen, Denmark.
Department of Chemistry - BMC, Uppsala University, Box 576, Husargatan 3, Uppsala, Sweden.
The Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Faculty of Health and Medical Sciences, Blegdamsvej 3B, Copenhagen, Denmark.
Umeå University, Faculty of Medicine, Department of Clinical Microbiology. Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).
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2021 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 12, no 1, article id 6761Article in journal (Refereed) Published
Abstract [en]

Viral proteins make extensive use of short peptide interaction motifs to hijack cellular host factors. However, most current large-scale methods do not identify this important class of protein-protein interactions. Uncovering peptide mediated interactions provides both a molecular understanding of viral interactions with their host and the foundation for developing novel antiviral reagents. Here we describe a viral peptide discovery approach covering 23 coronavirus strains that provides high resolution information on direct virus-host interactions. We identify 269 peptide-based interactions for 18 coronaviruses including a specific interaction between the human G3BP1/2 proteins and an ΦxFG peptide motif in the SARS-CoV-2 nucleocapsid (N) protein. This interaction supports viral replication and through its ΦxFG motif N rewires the G3BP1/2 interactome to disrupt stress granules. A peptide-based inhibitor disrupting the G3BP1/2-N interaction dampened SARS-CoV-2 infection showing that our results can be directly translated into novel specific antiviral reagents.

Place, publisher, year, edition, pages
Nature Publishing Group, 2021. Vol. 12, no 1, article id 6761
National Category
Infectious Medicine
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URN: urn:nbn:se:umu:diva-189992DOI: 10.1038/s41467-021-26498-zISI: 000720682600011Scopus ID: 2-s2.0-85119493526OAI: oai:DiVA.org:umu-189992DiVA, id: diva2:1615482
Funder
EU, Horizon 2020Swedish Foundation for Strategic Research , SB16-0039Knut and Alice Wallenberg FoundationSwedish Research Council, 2018-03843Swedish Research Council, 2018-05851Available from: 2021-11-30 Created: 2021-11-30 Last updated: 2023-09-05Bibliographically approved

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Lindquist, RichardNilsson, EmmaÖverby, Anna K.

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