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| Item Type: | Article |
|---|---|
| Title: | Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities |
| Creators Name: | 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., Överby, A.K., Nilsson, J. and Ivarsson, Y. |
| 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. |
| Keywords: | Signal Transducing Adaptor Proteins, DNA Helicases, Integration Host Factors, Poly-ADP-Ribose Binding Proteins, RNA Helicases, RNA Recognition Motif Proteins, RNA-Binding Proteins, SARS-CoV-2, Virus Replication / Physiology |
| Source: | Nature Communications |
| ISSN: | 2041-1723 |
| Publisher: | Nature Publishing Group |
| Volume: | 12 |
| Number: | 1 |
| Page Range: | 6761 |
| Date: | 19 November 2021 |
| Official Publication: | https://doi.org/10.1038/s41467-021-26498-z |
| PubMed: | View item in PubMed |
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