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Authors
Schmidt, NoraLareau, Caleb A
Keshishian, Hasmik
Ganskih, Sabina
Schneider, Cornelius
Hennig, Thomas
Melanson, Randy
Werner, Simone
Wei, Yuanjie
Zimmer, Matthias
Ade, Jens
Kirschner, Luisa
Zielinski, Sebastian
Dölken, Lars
Lander, Eric S
Caliskan, Neva
Fischer, Utz
Vogel, Jörg
Carr, Steven A
Bodem, Jochen
Munschauer, Mathias
Issue Date
2020-12-21
Metadata
Show full item recordAbstract
Characterizing the interactions that SARS-CoV-2 viral RNAs make with host cell proteins during infection can improve our understanding of viral RNA functions and the host innate immune response. Using RNA antisense purification and mass spectrometry, we identified up to 104 human proteins that directly and specifically bind to SARS-CoV-2 RNAs in infected human cells. We integrated the SARS-CoV-2 RNA interactome with changes in proteome abundance induced by viral infection and linked interactome proteins to cellular pathways relevant to SARS-CoV-2 infections. We demonstrated by genetic perturbation that cellular nucleic acid-binding protein (CNBP) and La-related protein 1 (LARP1), two of the most strongly enriched viral RNA binders, restrict SARS-CoV-2 replication in infected cells and provide a global map of their direct RNA contact sites. Pharmacological inhibition of three other RNA interactome members, PPIA, ATP1A1, and the ARP2/3 complex, reduced viral replication in two human cell lines. The identification of host dependency factors and defence strategies as presented in this work will improve the design of targeted therapeutics against SARS-CoV-2.Citation
Nat Microbiol. 2020 Dec 21. doi: 10.1038/s41564-020-00846-z. Epub ahead of print.Affiliation
HIRI, Helmholtz-Institut für RNA-basierte Infektionsforschung, Josef-Shneider Strasse 2, 97080 Würzburg, Germany.Publisher
Nature researchJournal
Nature microbiologyPubMed ID
33349665Type
ArticleLanguage
enEISSN
2058-5276ae974a485f413a2113503eed53cd6c53
10.1038/s41564-020-00846-z
Scopus Count
The following license files are associated with this item:
- Creative Commons
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