Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The garlic compound allicin causes strong disulfide stress and protein S-sulfoallylation as revealed by proteomics and transcriptomics in Staphylococcus aureus

ABSTRACT: Allicin from garlic is an antimicrobial substance that is effective against several ESKAPE pathogens, including methicillin-resistant Staphylococcus aureus (MRSA). However, the antimicrobial mode action of allicin has not been revealed in Gram-positive bacteria. Here, we have studied the changes in the transcriptome by Allicin which revealed a thiol-specific oxidative stress response in S. aureus. Using shotgun proteomics, we identified numerous proteins that were modified by protein S-sulfoallylation in S. aureus. Allicin further caused an oxidative shift in the bacillithiol (BSH) redox potential as revealed by Brx-roGFP2 biosensor measurements. In summary, our results revealed that allicin acts via sulfoallylation of Cys residues in proteins causing an impaired redox state in S. aureus.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Staphylococcus Aureus

SUBMITTER: Tobias Busche

LAB HEAD: Haike Antelmann

PROVIDER: PXD010338 | Pride | 2022-02-28

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	150409_V2_PM3_SK_HA_alicin_1_01.raw	Raw
	150409_V2_PM3_SK_HA_alicin_1_02.raw	Raw
	150409_V2_PM3_SK_HA_alicin_1_03.raw	Raw
	150409_V2_PM3_SK_HA_alicin_1_04.raw	Raw
	150409_V2_PM3_SK_HA_alicin_1_05.raw	Raw

Items per page:

1 - 5 of 27

Similar Datasets

The global effect of the garlic compound Allicin on the changes in the transcriptome in Bacillus subtilis and Staphylococcus aureus USA300 analysed by RNA-seq of coding RNA

Project description:To monitor the global changes in gene expression of Staphylococcus aureus USA300 TCH1516 under exposure to the garlic compound Allicin by RNA-seq, cultivation was performed in shaking flasks in Luria Bertani (LB) medium in triplicate at 37C until cells have reached an optical density at 540nm of 2.0. Cells were harvested by centrifugation, washed with Belitsky minimal medium (BMM) and adapted to BMM for one hour before exposure to 300 M Allicin stress. S. aureus cells of 3 replicate experiments were harvested before and 30 min after exposure to 300 M Allicin and disrupted in 3 mM EDTA/ 200 mM NaCl lysis buffer with a Precellys24 Ribolyzer. RNA isolation was performed using the phenol-chloroform-isoamylalcohol approach. After precipitation with 3 M sodium acetate and isopropanol, the total RNA was washed with cold ethanol and the pellet was solved in sterile water. Initially RNA quality was checked by Trinean Xpose (Gentbrugge,Belgium) and Agilent RNA Nano 6000 kit on Agilent 2100 Bioanalyzer (Agilent Technologies, Bblingen, Germany). Samples contaminated with DNA were treated with DNase (Qiagen), cleaned as described above and rechecked by Xpose and Agilent Bioanalyzer. Finally RNA was free of DNA with an RNA Integrity Number (RIN) > 9 and rRNA Ratio [23s / 16s] > 1.5. Ribo-Zero rRNA Removal Kit (Bacteria) from Illumina (San Diego, CA, USA) was used to remove the ribosomal RNA molecules from the isolated total RNA. Removal of rRNA was checked by Agilent RNA Pico 6000 kit on Agilent 2100 Bioanalyzer (Agilent Technologies, Bblingen, Germany). RNA was free of detectable rRNA. TruSeq Stranded mRNA Library Prep Kit from Illumina (San Diego, CA, USA) was used to prepare cDNA libraries. The resulting cDNAs were sequenced paired end on an Illumina MiSeq system (San Diego, CA, USA) using 75 bp read length.

2019-04-01 | E-MTAB-5667 | biostudies-arrayexpress

The sulfur stress response and protein S-thioallylation caused by allicin and diallyl polysulfanes in Bacillus subtilis as revealed by transcriptomics and proteomics

Project description:In this study, we compared the transcriptome signatures under allicin and diallyl tetrasulfane (DAS4) exposure in the Gram-positive bacterium B. subtilis. We further used shotgun proteomics to unravel the overall S-thioallylomes provoked by allicin and DAS4. Allicin and DAS4 caused a similar thiol-specific oxidative and electrophile stress response, protein and DNA damage in the transcriptome. At the proteome level, we identified in total 108 S-thioallylated proteins under allicin and/or DAS4 stress, while allicin appeared to have a stronger thiolation affect on redox-sensitive proteins. The S-thioallylome includes enzymes involved in the biosynthesis of surfactin (SrfAA, SrfAB), amino acids (SerA, MetE, YxjG, YitJ, CysJ, GlnA, YwaA), nucleotides (PurB, PurC, PyrAB, GuaB), translation factors (EF-Tu, EF-Ts, EF-G), antioxidant enzymes (AhpC, MsrB) as well as redox-sensitive MarR/OhrR and DUF24-family regulators (OhrR, HypR, YodB, CatR). Growth phenotype analysis revealed that the LMW thiol bacillithiol, the thiol-redox regulator Spx as well as the HypR and OhrR regulons confer protection against allicin and DAS4 stress. Altogether, we could show here that allicin and DAS4 cause both an oxidative and sulfur stress response in the transcriptome and widespread S-thioallylation of redox-sensitive proteins in B. subtilis.

2019-12-09 | PXD013607 | Pride

5'-RNAseq of 5'-enriched primary coding RNA in Staphylococcus aureus wildtype under 30 min allicin stress to detect Transcription Start Sites

Project description:To detect Transcription Start sites (TSS) in Staphylococcus aureus a cDNA library enriched for primary 5′-transcripts according to Peifer-Sancar et al. (2013) was prepared and sequenced on Illumina MiSeq system to retrieve 5′-ends of primary transcripts. Cultivation was performed in Luria Bertani (LB) medium in triplicate at 37°C until cells have reached an optical density at 540 nm of 2.0. Cells were harvested by centrifugation, washed with Belitsky minimal medium (BMM) and adapted to BMM for one hour. S. aureus cells of 3 replicate experiments were harvested before and 30 min after exposure to 300 µM allicin and disrupted in 3 mM EDTA/ 200 mM NaCl lysis buffer with a Precellys24 Ribolyzer. RNA isolation was performed using the phenol-chloroform-isoamylalcohol approach. After precipitation with 3 M sodium acetate and isopropanol, the total RNA was washed with cold ethanol and the pellet was solved in sterile water. Initially RNA quality was checked by Trinean Xpose (Gentbrugge,Belgium) and Agilent RNA Nano 6000 kit on Agilent 2100 Bioanalyzer (Agilent Technologies, Böblingen, Germany). Samples contaminated with DNA were treated with DNase (Qiagen), cleaned as described above and rechecked by Xpose and Agilent Bioanalyzer. Finally RNA was free of DNA with an RNA Integrity Number (RIN) > 9 and rRNA Ratio [23s / 16s] > 1.5. Ribo-Zero rRNA Removal Kit (Bacteria) from Illumina (San Diego, CA, USA) was used to remove the ribosomal RNA molecules from the isolated total RNA. Removal of rRNA was checked by Agilent RNA Pico 6000 kit on Agilent 2100 Bioanalyzer (Agilent Technologies, Böblingen, Germany). RNA was free of detectable rRNA. The method from Peifer-Sancar et al. (2013) was used to prepare a cDNA library enriched for primary 5′-transcript. The resulting cDNAs were sequenced paired end on an Illumina MiSeq system (San Diego, CA, USA) using 75 bp read length.

2021-10-25 | E-MTAB-10889 | biostudies-arrayexpress

The human allicin-proteome: global protein S-thioallylation of by the garlic defence substance allicin and its biological effects

Project description:A single clove of edible garlic (Allium sativum L.) produces up to 5 mg of allicin (diallylthiosulfinate), a thiol-reactive sulfur-containing defence substance that gives injured garlic tissue its characteristic smell. Allicin induces apoptosis or necrosis in a dose-dependent manner but sublethal doses influence cellular metabolism and signalling cascades. Oxidation of protein thiols and depletion of the glutathione pool are thought to be responsible for allicin’s physiological effects. Here, we studied the effect of Allicin on post-translational thiol-modification in human Jurkat cells using shotgun LC-MS/MS analyses. We identified 332 proteins in the human Jurkat cell proteome that were modified by S-thioallylation which causes a mass shift of 72 Dalton on cysteines. Many S-thioallylated proteins are high abundant proteins, including the cytoskeletal proteins tubulin, actin, cofilin, filamin and plastin-2, the heat shock chaperones HSP90 and HSPA4, the glycolytic enzymes GAPDH, ALDOA, PKM as well the protein translation factor EEF2. We confirmed that Allicin disrupted the actin cytoskeleton in mouseL929 fibroblasts. Allicin further resulted in Zn2+ release from proteins and stimulated the Zn2+-dependent IL1-triggered release of IL2 in murine EL4 T-cells. Allicin further caused inhibition of enolase activity. In conclusion, our study revealed the overall extent of widespread S-thioallylation in the human Jurkat cell proteome after allicin exposure which affects essential cellular functions of selected allicin targets.

2018-11-30 | PXD010201 | Pride

Effects of the antibacterial compund Allicin from garlic on Escherichia coli

Project description: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. Here, we show that upon exposure to allicin, growth of Escherichia coli is strongly inhibited. Growth inhibition coincides with a significant drop of total sulfhydryl concentrations and induction of the heat shock and oxidative stress response. In contrast to diamide, a potent inducer of disulfide stress, allicin does not induce cystine bond formation in proteins such as cytoplasmically expressed alkaline phosphatase PhoA. We identified and quantified the allicin-induced modification S-allylmercapto-cysteine for a set of cytoplasmic proteins by using a combination of label-free mass spectrometry and differential OxICAT labeling. Activity of isocitrate lyase AceA, an S-allylmercapto-modified candidate protein, is largely inhibited by allicin treatment in vivo. Our results indicate that the mode of action of allicin is a combination of disturbance of the redox balance and inactivation of crucial metabolic enzymes.

2016-05-02 | PXD003063 | Pride

Allicin inhibits SARS-CoV-2 replication and abrogates the antiviral host response in the Calu-3 proteome

Project description:The Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) pandemic causes a major health burden. Garlic organosulfur compounds, such as the diallyl thiosulfinate allicin exert strong antimicrobial activity against various respiratory pathogens. Here, we investigated the antiviral activity of allicin against SARS-CoV-2 in infected Vero E6 and Calu-3 lung cells. Allicin efficiently inhibited viral replication and infectivity in both cell lines. Proteome analyses of infected Calu-3 cells revealed a strong induction of the antiviral interferon-stimulated gene (ISG) signature (e.g. Mx1, IFIT, 2’5’OAS and ISG15), pathways of vesicular transport, tight junctions (KIF5A/B/C, OSBPL2, CLTC1, ARHGAP17) and ubiquitin modification (UBE2L3/5), as well as reprogramming of host metabolism, transcription and translation. Allicin abrogated the ISG host response and reverted the host cellular pathways to Mock levels, confirming the antiviral and immunomodulatory activity of allicin in the host proteome. Thus, biocompatible doses of garlic could be promising for protection of lung cells against SARS-CoV-2.

2021-06-30 | PXD024375 | Pride

The global effect of hypochlorite stress on the changes in the transcriptome in Staphylococcus aureus USA300

Project description:To monitor the global changes in gene expression of Staphylococcus aureus USA300 TCH1516 under hypochlorite stress by RNA-seq, cultivation was performed in Luria Bertani (LB) medium in triplicate at 37C until cells have reached an optical density at 540nm of 2.0. Cells were harvested by centrifugation, washed with Belitsky minimal medium (BMM) and adapted to BMM for one hour before exposure to 150 M NaOCl stress. S. aureus cells of 3 replicate experiments were harvested before and 30 min after exposure to 150 M NaOCl and disrupted in 3 mM EDTA/ 200 mM NaCl lysis buffer with a Precellys24 Ribolyzer. RNA isolation was performed using the phenol-chloroform-isoamylalcohol approach. After precipitation with 3 M sodium acetate and isopropanol, the total RNA was washed with cold ethanol and the pellet was solved in sterile water. Initially RNA quality was checked by Trinean Xpose (Gentbrugge,Belgium) and Agilent RNA Nano 6000 kit on Agilent 2100 Bioanalyzer (Agilent Technologies, Bblingen, Germany). Samples contaminated with DNA were treated with DNase (Qiagen), cleaned as described above and rechecked by Xpose and Agilent Bioanalyzer. Finally RNA was free of DNA with an RNA Integrity Number (RIN) > 9 and rRNA Ratio [23s / 16s] > 1.5. Ribo-Zero rRNA Removal Kit (Bacteria) from Illumina (San Diego, CA, USA) was used to remove the ribosomal RNA molecules from the isolated total RNA. Removal of rRNA was checked by Agilent RNA Pico 6000 kit on Agilent 2100 Bioanalyzer (Agilent Technologies, Bblingen, Germany). RNA was free of detectable rRNA. TruSeq Stranded mRNA Library Prep Kit from Illumina (San Diego, CA, USA) was used to prepare cDNA libraries. The resulting cDNAs were sequenced paired end on an Illumina HiSeq 1500 and MiSeq system (San Diego, CA, USA) using 50 and 75 bp read length, respectively.

2017-12-18 | E-MTAB-5666 | biostudies-arrayexpress

Effects of the antibacterial compund Allicin from garlic on Escherichia coli

2016-03-29 | PXD003158 | Pride

Expression data from Staphylococcus aureus ATCC 25923 (antibiotic sensitive) and ATCC 33591 (MRSA)

Project description:S. aureus ATCC 25923 is performance standard for antimicrobial susceptibility testing. S. aureus ATCC 33591 showed resistance against erytrhromycin, penicillin, and streptomycin. We used microarray to compare RNA expression between sensitive and resistant strain of S. aureus as a preliminary research for MRSA inhibition. S. aureus strains were cultivated in tryptic soy broth at 37℃ for 18hrs and harvested for RNA extraction and hybridization on Affymetrix microarrays.

2010-09-15 | E-GEOD-18289 | biostudies-arrayexpress

Interspecies comparison of the bacterial response to allicin reveals species-specific defense strategies

Project description:Allicin, a volatile diallylthiosulfinate from garlic (Allium sativum), exhibits broad-spectrum activity against microbial pathogens. It disrupts thiol and redox homeostasis, proteostasis, and cell membrane integrity leading to inactivation of even multidrug resistant strains. Since medicine demands cost-efficient antimicrobials with so far unexploited mechanisms, allicin with its multifaceted mode of action is a promising lead structure for future therapeutics. However, while progress is being made in fully unraveling its mode of action, little is known on bacterial adaptation strategies to cope with allicin-like stress. Some isolates of Pseudomonas aeruginosa and Escherichia coli, withstand exposure to higher allicin concentrations than other bacteria due to as yet unknown cellular mechanisms. To elucidate resistance and sensitivity-conferring cellular processes we compared the acute proteomic responses of the resistant species P. aeruginosa and sensitive species Bacillus subtilis to the published proteomic response of E. coli to allicin treatment. The cellular defense strategies shared functional features: proteins involved in protein (re)folding and repair, ROS and RSS detoxification, and cell envelope modification were upregulated. In both Gram-negative species, protein synthesis of up to 64% of the proteins synthesized in untreated cells was down-regulated while the sensitive, Gram-positive B. subtilis responded by upregulation of multiple regulons. A comparison of the B. subtilis proteomic response to a library of proteomic responses to antibiotic treatment, revealed 30 proteins specifically upregulated by allicin. Other upregulated proteins indicating oxidative stress were shared with nitrofurantoin and diamide. Microscopy-based assays further indicate that in B. subtilis cell wall integrity was impaired.

2021-03-09 | PXD012622 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data