Evidence map›Paper›PMID 27008862›Full record

ArticleThe Journal of biological chemistry2016

Allicin Induces Thiol Stress in Bacteria through S-Allylmercapto Modification of Protein Cysteines.

Alexandra Müller, Jakob Eller, Frank Albrecht, Pascal Prochnow, Katja Kuhlmann, Julia Elisabeth Bandow, Alan John Slusarenko, Lars Ingo Ole Leichert

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
30.2field-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

69 citing papers in PubMed, 161 citations in OpenAlex.

  1. Journal of gastrointestinal oncology · 2026
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  11. Modification of human metallothioneins by garlic organosulfur compounds, allicin and ajoene: direct effect on zinc homeostasis with relevance to immune regulation.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025
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9 more citing papers are in PubMed but not listed here.

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

8 authors at 4 institutions in 2 countries.

Alexandra MüllerFrom the Institute of Biochemistry and Pathobiochemistry-Microbial Biochemistry.
Jakob EllerFrom the Institute of Biochemistry and Pathobiochemistry-Microbial Biochemistry.
Frank AlbrechtDepartment of Plant Physiology, Rheinisch-Westfälische Technische Hochschule Aachen University, 52056 Aachen, Germany.
Pascal ProchnowAngewandte Mikrobiologie, and.
Katja KuhlmannMedizinisches Proteom-Center, Ruhr University Bochum, 44780 Bochum, Germany and.
Julia Elisabeth BandowAngewandte Mikrobiologie, and.
Alan John SlusarenkoDepartment of Plant Physiology, Rheinisch-Westfälische Technische Hochschule Aachen University, 52056 Aachen, Germany.
Lars Ingo Ole LeichertFrom the Institute of Biochemistry and Pathobiochemistry-Microbial Biochemistry, lars.leichert@ruhr-uni-bochum.de.ORCID 0000-0002-5666-9681
Institut für angewandte Photonik · DEMicrobial Chemistry Research Foundation · JPRuhr University Bochum · DERWTH Aachen University · DE

Funding

European Research Council 281384
6 · The paper itself

Abstract

Allicin (diallyl thiosulfinate) from garlic is a highly potent natural antimicrobial substance. It inhibits growth of a variety of microorganisms, among them antibiotic-resistant strains. However, the precise mode of action of allicin is unknown. Here, we show that growth inhibition of Escherichia coli during allicin exposure coincides with a depletion of the glutathione pool and S-allylmercapto modification of proteins, resulting in overall decreased total sulfhydryl levels. This is accompanied by the induction of the oxidative and heat stress response. We identified and quantified the allicin-induced modification S-allylmercaptocysteine for a set of cytoplasmic proteins by using a combination of label-free mass spectrometry and differential isotope-coded affinity tag labeling of reduced and oxidized thiol residues. Activity of isocitrate lyase AceA, an S-allylmercapto-modified candidate protein, is largely inhibited by allicin treatment in vivo Allicin-induced protein modifications trigger protein aggregation, which largely stabilizes RpoH and thereby induces the heat stress response. At sublethal concentrations, the heat stress response is crucial to overcome allicin stress. Our results indicate that the mode of action of allicin is a combination of a decrease of glutathione levels, unfolding stress, and inactivation of crucial metabolic enzymes through S-allylmercapto modification of cysteines.

Indexed as

CysteineDisulfidesEscherichia coliEscherichia coli ProteinsGarlicGlutathionePlant ExtractsProtein Processing, Post-TranslationalSulfhydryl CompoundsSulfinic AcidsallicinCysteineDisulfidesEscherichia coli ProteinsGlutathionePlant ExtractsSulfhydryl CompoundsSulfinic Acidsallicinantibiotic actionbacteriadisulfideEscherichia coli (E. coli)garlic (Allium sativum)redox proteomicsS-allylmercapto modificationthiol

Identifiers

PMID27008862
PMCPMC4882420
OpenAlexW2303633006

What OpenQuestion holds

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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.