SARS-CoV-2 hijacks a cell damage response, which induces transcription of a more efficient Spike S-acyltransferase

Francisco S. Mesquita (), Laurence Abrami, Lucie Bracq, Nattawadee Panyain, Vincent Mercier, Béatrice Kunz, Audrey Chuat, Joana Carlevaro-Fita, Didier Trono and F. Gisou van der Goot ()
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Francisco S. Mesquita: School of Life Sciences, EPFL
Laurence Abrami: School of Life Sciences, EPFL
Lucie Bracq: School of Life Sciences, EPFL
Nattawadee Panyain: School of Life Sciences, EPFL
Vincent Mercier: School of Life Sciences, EPFL
Béatrice Kunz: School of Life Sciences, EPFL
Audrey Chuat: School of Life Sciences, EPFL
Joana Carlevaro-Fita: School of Life Sciences, EPFL
Didier Trono: School of Life Sciences, EPFL
F. Gisou van der Goot: School of Life Sciences, EPFL

Nature Communications, 2023, vol. 14, issue 1, 1-17

Abstract: Abstract SARS-CoV-2 infection requires Spike protein-mediated fusion between the viral and cellular membranes. The fusogenic activity of Spike depends on its post-translational lipid modification by host S-acyltransferases, predominantly ZDHHC20. Previous observations indicate that SARS-CoV-2 infection augments the S-acylation of Spike when compared to mere Spike transfection. Here, we find that SARS-CoV-2 infection triggers a change in the transcriptional start site of the zdhhc20 gene, both in cells and in an in vivo infection model, resulting in a 67-amino–acid-long N-terminally extended protein with approx. 40 times higher Spike acylating activity, resulting in enhanced fusion of viruses with host cells. Furthermore, we observed the same induced transcriptional change in response to other challenges, such as chemically induced colitis and pore-forming toxins, indicating that SARS-CoV-2 hijacks an existing cell damage response pathway to optimize it fusion glycoprotein.

Date: 2023
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DOI: 10.1038/s41467-023-43027-2

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