About: A direct RNA-protein interaction atlas of the SARS-CoV-2 RNA in infected human cells

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About: A direct RNA-protein interaction atlas of the SARS-CoV-2 RNA in infected human cells Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	A direct RNA-protein interaction atlas of the SARS-CoV-2 RNA in infected human cells
Creator	Caliskan, Neva Schmidt, Nora Affiliations, § Lander, Eric Ade, Jens Bodem, Jochen Carr, Steven Keshishian, Hasmik Kirschner, Luisa Lareau, Caleb Melanson, Randy Munschauer, Mathias Vogel, Jörg Werner, Simone Zimmer, Matthias
Source	BioRxiv
abstract	SARS-CoV-2 infections pose a global threat to human health and an unprecedented research challenge. Among the most urgent tasks is obtaining a detailed understanding of the molecular interactions that facilitate viral replication or contribute to host defense mechanisms in infected cells. While SARS-CoV-2 co-opts cellular factors for viral translation and genome replication, a comprehensive map of the host cell proteome in direct contact with viral RNA has not been elucidated. Here, we use RNA antisense purification and mass spectrometry (RAP-MS) to obtain an unbiased and quantitative picture of the human proteome that directly binds the SARS-CoV-2 RNA in infected human cells. We discover known host factors required for coronavirus replication, regulators of RNA metabolism and host defense pathways, along with dozens of potential drug targets among direct SARS-CoV-2 binders. We further integrate the SARS-CoV-2 RNA interactome with proteome dynamics induced by viral infection, linking interactome proteins to the emerging biology of SARS-CoV-2 infections. Validating RAP-MS, we show that CNBP, a regulator of proinflammatory cytokines, directly engages the SARS-CoV-2 RNA. Supporting the functional relevance of identified interactors, we show that the interferon-induced protein RYDEN suppresses SARS-CoV-2 ribosomal frameshifting and demonstrate that inhibition of SARS-CoV-2-bound proteins is sufficient to manipulate viral replication. The SARS-CoV-2 RNA interactome provides an unprecedented molecular perspective on SARS-CoV-2 infections and enables the systematic dissection of host dependency factors and host defense strategies, a crucial prerequisite for designing novel therapeutic strategies.
has issue date	2020-07-15(xsd:dateTime)
bibo:doi	10.1101/2020.07.15.204404
has license	biorxiv
sha1sum (hex)	5c27876dd85f551d53138d9af31a208c763f7b0a
schema:url	https://doi.org/10.1101/2020.07.15.204404
resource representing a document's title	A direct RNA-protein interaction atlas of the SARS-CoV-2 RNA in infected human cells
schema:publication	bioRxiv
resource representing a document's body	covid:5c27876dd85f551d53138d9af31a208c763f7b0a#body_text
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