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

The fusogenic activity of SARS-CoV-2 Spike depends on its post-translational lipid modification by host S-acyltransferases, predominantly ZDHHC20. Here, Mesquita and Abrami et al. show that SARS-CoV-2 infection and colitis in mice induce a damage response resulting in an altered version of the ZDHHC20 enzyme that is more abundant and significantly more efficient at attaching fatty acids to viral Spike.

Francisco S. Mesquita
Laurence Abrami
F. Gisou van der Goot
ResearchOpen Access11 Nov 2023
Nature Communications

Volume: 14, P: 1-17
Dual chemical probes enable quantitative system-wide analysis of protein prenylation and prenylation dynamics

Two chemical probes, YnF and YnGG, that enable the identification of prenylated peptides and global analysis of protein prenylation using quantitative chemical proteomics have now been developed. Prenylation dynamics in response to pharmacological inhibition of prenyl-transferase enzymes were also studied. As a final demonstration, defective Rab prenylation in a model of the retinal degenerative disease choroideremia was also quantified.

Elisabeth M. Storck
Julia Morales-Sanfrutos
Edward W. Tate
Research01 Apr 2019
Nature Chemistry

Volume: 11, P: 552-561
Proteome-wide analysis of protein lipidation using chemical probes: in-gel fluorescence visualization, identification and quantification of N-myristoylation, N- and S-acylation, O-cholesterylation, S-farnesylation and S-geranylgeranylation

Protein lipidation is challenging to analyze on the proteome level. This protocol describes metabolic incorporation of lipid probes and their capture via click chemistry, allowing in-gel fluorescence visualization or mass spectrometry analysis.

Wouter W. Kallemeijn
Thomas Lanyon-Hogg
Edward W. Tate
Protocols27 Oct 2021
Nature Protocols

Volume: 16, P: 5083-5122

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

Dual chemical probes enable quantitative system-wide analysis of protein prenylation and prenylation dynamics

Proteome-wide analysis of protein lipidation using chemical probes: in-gel fluorescence visualization, identification and quantification of N-myristoylation, N- and S-acylation, O-cholesterylation, S-farnesylation and S-geranylgeranylation

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