About: TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells

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About: TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells
Creator	Eickmann, Markus Böttcher-Friebertshäuser, Eva Klenk, Hans-Dieter Garten, Wolfgang Dolnik, Olga Rohde, Cornelius Moulton, Hong Stein, David Hardes, Kornelia Steinmetzer, Torsten Bestle, Dorothea Limburg, Hannah Pilgram, Oliver Lam Van, Thuy Ruth Heindl, Miriam
Source	Medline; PMC
abstract	The novel emerged SARS-CoV-2 has rapidly spread around the world causing acute infection of the respiratory tract (COVID-19) that can result in severe disease and lethality. For SARS-CoV-2 to enter cells, its surface glycoprotein spike (S) must be cleaved at two different sites by host cell proteases, which therefore represent potential drug targets. In the present study, we show that S can be cleaved by the proprotein convertase furin at the S1/S2 site and the transmembrane serine protease 2 (TMPRSS2) at the S2′ site. We demonstrate that TMPRSS2 is essential for activation of SARS-CoV-2 S in Calu-3 human airway epithelial cells through antisense-mediated knockdown of TMPRSS2 expression. Furthermore, SARS-CoV-2 replication was also strongly inhibited by the synthetic furin inhibitor MI-1851 in human airway cells. In contrast, inhibition of endosomal cathepsins by E64d did not affect virus replication. Combining various TMPRSS2 inhibitors with furin inhibitor MI-1851 produced more potent antiviral activity against SARS-CoV-2 than an equimolar amount of any single serine protease inhibitor. Therefore, this approach has considerable therapeutic potential for treatment of COVID-19.
has issue date	2020-07-23(xsd:dateTime)
bibo:doi	10.26508/lsa.202000786
bibo:pmid	32703818
has license	cc-by
sha1sum (hex)	cfc4ff061a07e619bdf447d06463b252d75c685a
schema:url	https://doi.org/10.26508/lsa.202000786
resource representing a document's title	TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells
has PubMed Central identifier	PMC7383062
has PubMed identifier	32703818
schema:publication	Life Sci Alliance
resource representing a document's body	covid:cfc4ff061a07e619bdf447d06463b252d75c685a#body_text
is schema:about of	named entity 'potential' named entity 'site' named entity 'cleaved' named entity 'cathepsins' named entity 'Combining' named entity 'antiviral' named entity 'S29' named entity 'serine protease inhibitor' named entity 'furin' named entity 'epithelial cells' named entity 'drug targets' named entity 'SARS-CoV-2' named entity 'TMPRSS2' named entity 'SARS-CoV-2' named entity 'S29' named entity 'cell cultures' named entity 'trypsin' named entity 'avian infectious bronchitis virus' named entity 'SARS-CoV' named entity 'hydrophobic' named entity 'furin' named entity 'TMPRSS2' named entity 'complementary sequence' named entity 'furin' named entity 'cathepsin' named entity 'protein' named entity 'influenza A virus' named entity 'fusion proteins' named entity 'amide' named entity 'furin' named entity 'TMPRSS2' named entity 'proteolytic' named entity 'FRET' named entity 'primers' named entity 'Calu-3' named entity 'furin' named entity 'S29' named entity 'inhalation' named entity 'furin' named entity 'COVID' named entity 'IBV' named entity 'protein' named entity 'inhalation' named entity 'motif' named entity 'growth factors' named entity 'S29' named entity 'SARS-CoV-2' named entity 'S29' named entity 'human coronaviruses' named entity 'drug repurposing' named entity 'furin' named entity 'virus entry' named entity 'serine proteases' named entity 'antiviral activity' named entity 'furin' named entity 'SARS-CoV-2' named entity 'pancreatitis' named entity 'TMPRSS2' named entity 'TMPRSS2' named entity 'aprotinin' named entity 'antisense' named entity 'plasmid' named entity 'TMPRSS2' named entity 'TMPRSS2' named entity 'proteolytic' named entity 'TMPRSS2' named entity 'exon skipping'

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