Evidence map›Paper›PMID 34599882›Full record

ArticleDevelopmental cell2021

S-acylation controls SARS-CoV-2 membrane lipid organization and enhances infectivity.

Francisco S Mesquita, Laurence Abrami, Oksana Sergeeva, Priscilla Turelli, Enya Qing, Béatrice Kunz, Charlène Raclot, Jonathan Paz Montoya, Luciano A Abriata, Tom Gallagher and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Developmental cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
8.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

94 citing papers in PubMed, 128 citations in OpenAlex.

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  8. Palmitoylated COX-2Journal of advanced research · 2026
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34 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 2 institutions in 2 countries.

Francisco S MesquitaGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland. Electronic address: francisco.mesquita@epfl.ch.
Laurence AbramiGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland.
Oksana SergeevaGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland.
Priscilla TurelliGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland.
Enya QingDepartment of Microbiology and Immunology, Loyola University Chicago, Maywood, IL, USA.
Béatrice KunzGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland.
Charlène RaclotGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland.
Jonathan Paz MontoyaInstitute of Bioengineering, School of Life Sciences, EPFL, Lausanne, Switzerland.
Luciano A AbriataInstitute of Bioengineering, School of Life Sciences, EPFL, Lausanne, Switzerland.
Tom GallagherDepartment of Microbiology and Immunology, Loyola University Chicago, Maywood, IL, USA.
Matteo Dal PeraroInstitute of Bioengineering, School of Life Sciences, EPFL, Lausanne, Switzerland.
Didier TronoGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland.
Giovanni D'AngeloInstitute of Bioengineering, School of Life Sciences, EPFL, Lausanne, Switzerland.
F Gisou van der GootGlobal Health Institute, School of Life Sciences, EPFL, Lausanne, Switzerland. Electronic address: gisou.vandergoot@epfl.ch.
École Polytechnique Fédérale de Lausanne · CHLoyola University Chicago · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SARS-CoV-2 virions are surrounded by a lipid bilayer that contains membrane proteins such as spike, responsible for target-cell binding and virus fusion. We found that during SARS-CoV-2 infection, spike becomes lipid modified, through the sequential action of the S-acyltransferases ZDHHC20 and 9. Particularly striking is the rapid acylation of spike on 10 cytosolic cysteines within the ER and Golgi. Using a combination of computational, lipidomics, and biochemical approaches, we show that this massive lipidation controls spike biogenesis and degradation, and drives the formation of localized ordered cholesterol and sphingolipid-rich lipid nanodomains in the early Golgi, where viral budding occurs. Finally, S-acylation of spike allows the formation of viruses with enhanced fusion capacity. Our study points toward S-acylating enzymes and lipid biosynthesis enzymes as novel therapeutic anti-viral targets.

Indexed as

COVID-19 Drug TreatmentAcylationAcyltransferasesGolgi ApparatusHumansMembrane LipidsSARS-CoV-2Virus AssemblyAcyltransferasesMembrane LipidsZDHHC20 protein, humancoronaviruslipid microdomainslipid sortingSARSS-palmitoylationspikeviral envelopevirusZDHHC

Identifiers

PMID34599882
PMCPMC8486083
OpenAlexW3201877532

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.