What is it about?

The S1/S2 cleavage site of the SARS-CoV-2 spike protein contains several arginine residues and is not found in closely related coronaviruses. Here, we show that this site is cleaved by the cellular protease furin and that cleavage is required for infection of lung cells.

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Why is it important?

Our present and previous study revealed how SARS-CoV-2 is activated by cellular proteases for entry into lung cells. The spike protein has to be cleaved by furin in infected cells for subsequent cleavage and activation by TMPRSS2 for entry into lung cells. Therefore, both furin and TMPRSS2 are potential therapeutic targets.


It will be interesting to determine whether furin and TMPRSS2 inhibitors inhibit SARS-CoV-2 infection and COVID-19. Clinical trials analyzing the antiviral activity of the TMPRSS2 inhibitor camostat mesylate are already under way.

Professor Stefan Pöhlmann
German Primate Center

Read the Original

This page is a summary of: A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells, Molecular Cell, May 2020, Elsevier, DOI: 10.1016/j.molcel.2020.04.022.
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