Evidence map›Paper›PMID 35336938›Full record

ArticleViruses2022

Identification of SARS-CoV-2 Spike Palmitoylation Inhibitors That Results in Release of Attenuated Virus with Reduced Infectivity.

Ahmed A Ramadan, Karthick Mayilsamy, Andrew R McGill, Anandita Ghosh, Marc A Giulianotti, Haley M Donow, Shyam S Mohapatra, Subhra Mohapatra, Bala Chandran, Robert J Deschenes and 1 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Viruses, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.1field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Palmitoylated COX-2Journal of advanced research · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Ahmed A RamadanDepartment of Molecular Medicine, University of South Florida, Tampa, FL 33612, USA.
Karthick MayilsamyDepartment of Molecular Medicine, University of South Florida, Tampa, FL 33612, USA.
Andrew R McGillDepartment of Molecular Medicine, University of South Florida, Tampa, FL 33612, USA.
Anandita GhoshDepartment of Molecular Medicine, University of South Florida, Tampa, FL 33612, USA.
Marc A GiulianottiCenter for Translational Science, Florida International University, Port St. Lucie, FL 34987, USA.
Haley M DonowCenter for Translational Science, Florida International University, Port St. Lucie, FL 34987, USA.
Shyam S MohapatraDepartment of Molecular Medicine, University of South Florida, Tampa, FL 33612, USA.ORCID 0000-0001-5838-0681
Subhra MohapatraDepartment of Molecular Medicine, University of South Florida, Tampa, FL 33612, USA.
Bala ChandranDepartment of Molecular Medicine, University of South Florida, Tampa, FL 33612, USA.
Robert J DeschenesDepartment of Molecular Medicine, University of South Florida, Tampa, FL 33612, USA.
Arunava RoyDepartment of Molecular Medicine, University of South Florida, Tampa, FL 33612, USA.
University of South Florida · USFlorida International University · US

Funding

KSHV interactions with host nuclear innate response componentsR01CA180758 · NCI · UNIVERSITY OF SOUTH FLORIDA · PI CHANDRAN, BALA · 2014 to 2023
$3.4M
Protein Palmitoylation and the Etiology of X-Linked Intellectual DisabilitiesR21NS090160 · NINDS · UNIVERSITY OF SOUTH FLORIDA · PI DESCHENES, ROBERT J · 2016 to 2017
$411k
BLRD VA I01 BX005490BLRD VA IK6 BX004212NCI NIH HHS CA180758NCI NIH HHS R01 CA180758NINDS NIH HHS NS090160NINDS NIH HHS R21 NS090160
6 · The paper itself

Abstract

The spike proteins of enveloped viruses are transmembrane glycoproteins that typically undergo post-translational attachment of palmitate on cysteine residues on the cytoplasmic facing tail of the protein. The role of spike protein palmitoylation in virus biogenesis and infectivity is being actively studied as a potential target of novel antivirals. Here, we report that palmitoylation of the first five cysteine residues of the C-terminal cysteine-rich domain of the SARS-CoV-2 S protein are indispensable for infection, and palmitoylation-deficient spike mutants are defective in membrane fusion. The DHHC9 palmitoyltransferase interacts with and palmitoylates the spike protein in the ER and Golgi and knockdown of DHHC9 results in reduced fusion and infection of SARS-CoV-2. Two bis-piperazine backbone-based DHHC9 inhibitors inhibit SARS-CoV-2 S protein palmitoylation and the resulting progeny virion particles released are defective in fusion and infection. This establishes these palmitoyltransferase inhibitors as potential new intervention strategies against SARS-CoV-2.

Indexed as

COVID-19SARS-CoV-2HumansLipoylationSpike Glycoprotein, CoronavirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2antiviralbis-piperazineDHHC9palmitoylationpalmitoyltransferasepalmitoyltransferase inhibitorpost-translational modificationsS-acylationSARS-CoV-2spike

Identifiers

PMID35336938
PMCPMC8950683
OpenAlexW4220777057

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.