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Interaction Information:
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Comment
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The spike (S) protein of coronaviruses facilitates viral entry into target cells. Entry depends on binding of the surface unit, S1, of the S protein to a cellular receptor, which facilitates viral attachment to the surface of target cells. In addition, entry requires S protein priming by cellular proteases, which entails S protein cleavage at the S1/S2 and the S2’ site and allows fusion of viral and cellular membranes, a process driven by the S2 subunit. The goal of this study was to obtain insights into how SARS-2-S facilitates viral entry into target cells and how this process can be blocked. Directed expression of human and bat (Rhinolophus alcyone) ACE2 but not human DPP4, the entry receptor used by MERS-CoV, or human APN, the entry receptor used by HCoV-229E, allowed SARS-2-S- and SARS-S-driven entry into otherwise non-susceptible BHK-21 cells. Moreover, anti-serum raised against human ACE2 blocked SARS-S- andSARS-2-S- but not VSV-G- or MERS-S-driven entry. Finally, authentic SARS-CoV-2 infected BHK-21 cells transfected to express ACE2 cells but not parental BHK-21 cells with high efficiency, indicating that SARS-2-S, like SARS-S, uses ACE2 for cellular entry.
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Formal Description
Interaction-ID: 116824
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environment
SARS-CoV-2 S protein
interacts (colocalizes) with
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Drugbank entries
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Show/Hide entries for
ACE2
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Drugbank
DB00691
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Drugbank
DB00722
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Comment
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SARS-CoV can use the endosomal cysteine proteases cathepsin B and L (CatB/L) and the serineprotease TMPRSS2 for S protein priming in cell lines, and inhibition of both proteases is required for robust blockade of viral entry. However, only TMPRSS2 activity is essential for viral spread and pathogenesis in the infected host whereas CatB/L activity is dispensable. This study shows that SARS-CoV-2 can use TMPRSS2 for S protein priming and camostat mesylate, an inhibitor of TMPRSS2, blocks SARS-CoV-2 infection of lung cells.
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Formal Description
Interaction-ID: 116872
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environment
SARS-CoV-2 S protein
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Comment
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SARS-CoV can use the endosomal cysteine proteases cathepsin B and L (CatB/L) and the serineprotease TMPRSS2 for S protein priming in cell lines, and inhibition of both proteases is required for robust blockade of viral entry. However, only TMPRSS2 activity is essential for viral spread and pathogenesis in the infected host whereas CatB/L activity is dispensable. This study shows that SARS-CoV-2 can use TMPRSS2 for S protein priming and camostat mesylate, an inhibitor of TMPRSS2, blocks SARS-CoV-2 infection of lung cells.
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Formal Description
Interaction-ID: 116877
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CIDeR