Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities. / Kruse, Thomas; Benz, Caroline; Garvanska, Dimitriya H; Lindqvist, Richard; Mihalic, Filip; Coscia, Fabian; Inturi, Raviteja; Sayadi, Ahmed; Simonetti, Leandro; Nilsson, Emma; Ali, Muhammad; Kliche, Johanna; Moliner Morro, Ainhoa; Mund, Andreas; Andersson, Eva; McInerney, Gerald; Mann, Matthias; Jemth, Per; Davey, Norman E; Överby, Anna K; Nilsson, Jakob; Ivarsson, Ylva.

In: Nature Communications, Vol. 12, No. 1, 6761, 2021.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kruse, T, Benz, C, Garvanska, DH, Lindqvist, R, Mihalic, F, Coscia, F, Inturi, R, Sayadi, A, Simonetti, L, Nilsson, E, Ali, M, Kliche, J, Moliner Morro, A, Mund, A, Andersson, E, McInerney, G, Mann, M, Jemth, P, Davey, NE, Överby, AK, Nilsson, J & Ivarsson, Y 2021, 'Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities', Nature Communications, vol. 12, no. 1, 6761. https://doi.org/10.1038/s41467-021-26498-z

APA

Kruse, T., Benz, C., Garvanska, D. H., Lindqvist, R., Mihalic, F., Coscia, F., Inturi, R., Sayadi, A., Simonetti, L., Nilsson, E., Ali, M., Kliche, J., Moliner Morro, A., Mund, A., Andersson, E., McInerney, G., Mann, M., Jemth, P., Davey, N. E., ... Ivarsson, Y. (2021). Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities. Nature Communications, 12(1), [6761]. https://doi.org/10.1038/s41467-021-26498-z

Vancouver

Kruse T, Benz C, Garvanska DH, Lindqvist R, Mihalic F, Coscia F et al. Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities. Nature Communications. 2021;12(1). 6761. https://doi.org/10.1038/s41467-021-26498-z

Author

Kruse, Thomas ; Benz, Caroline ; Garvanska, Dimitriya H ; Lindqvist, Richard ; Mihalic, Filip ; Coscia, Fabian ; Inturi, Raviteja ; Sayadi, Ahmed ; Simonetti, Leandro ; Nilsson, Emma ; Ali, Muhammad ; Kliche, Johanna ; Moliner Morro, Ainhoa ; Mund, Andreas ; Andersson, Eva ; McInerney, Gerald ; Mann, Matthias ; Jemth, Per ; Davey, Norman E ; Överby, Anna K ; Nilsson, Jakob ; Ivarsson, Ylva. / Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities. In: Nature Communications. 2021 ; Vol. 12, No. 1.

Bibtex

@article{5c29c86bf4ca47f7bc8b6febe6a78d09,
title = "Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities",
abstract = "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.",
author = "Thomas Kruse and Caroline Benz and Garvanska, {Dimitriya H} and Richard Lindqvist and Filip Mihalic and Fabian Coscia and Raviteja Inturi and Ahmed Sayadi and Leandro Simonetti and Emma Nilsson and Muhammad Ali and Johanna Kliche and {Moliner Morro}, Ainhoa and Andreas Mund and Eva Andersson and Gerald McInerney and Matthias Mann and Per Jemth and Davey, {Norman E} and {\"O}verby, {Anna K} and Jakob Nilsson and Ylva Ivarsson",
note = "{\textcopyright} 2021. The Author(s).",
year = "2021",
doi = "10.1038/s41467-021-26498-z",
language = "English",
volume = "12",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities

AU - Kruse, Thomas

AU - Benz, Caroline

AU - Garvanska, Dimitriya H

AU - Lindqvist, Richard

AU - Mihalic, Filip

AU - Coscia, Fabian

AU - Inturi, Raviteja

AU - Sayadi, Ahmed

AU - Simonetti, Leandro

AU - Nilsson, Emma

AU - Ali, Muhammad

AU - Kliche, Johanna

AU - Moliner Morro, Ainhoa

AU - Mund, Andreas

AU - Andersson, Eva

AU - McInerney, Gerald

AU - Mann, Matthias

AU - Jemth, Per

AU - Davey, Norman E

AU - Överby, Anna K

AU - Nilsson, Jakob

AU - Ivarsson, Ylva

N1 - © 2021. The Author(s).

PY - 2021

Y1 - 2021

N2 - 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.

AB - 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.

U2 - 10.1038/s41467-021-26498-z

DO - 10.1038/s41467-021-26498-z

M3 - Journal article

C2 - 34799561

VL - 12

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 6761

ER -

ID: 285718968