<<< Full experiment listing

PXD012622

PXD012622 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleInterspecies comparison of the bacterial response to allicin reveals species-specific defense strategies
DescriptionAllicin, 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.
HostingRepositoryPRIDE
AnnounceDate2021-03-09
AnnouncementXMLSubmission_2021-03-09_05:23:50.548.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterChristoph Senges
SpeciesList scientific name: Bacillus subtilis subsp. subtilis str. 168; NCBI TaxID: 224308; scientific name: Pseudomonas aeruginosa PAO1; NCBI TaxID: 208964;
ModificationListmonohydroxylated residue; iodoacetamide derivatized residue; deamidated residue
InstrumentSynapt MS
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-02-07 23:56:49ID requested
12021-03-09 02:47:50announced
22021-03-09 05:23:51announced2021-03-09: Updated publication reference for PubMed record(s): 31622046.
Publication List
W, ΓΌ, llner D, Haupt A, Prochnow P, Leontiev R, Slusarenko AJ, Bandow JE, Interspecies Comparison of the Bacterial Response to Allicin Reveals Species-Specific Defense Strategies. Proteomics, 19(24):e1900064(2019) [pubmed]
Keyword List
curator keyword: Biological
submitter keyword: allicin, mode of action, proteomic response, Bacillus subtilis, Pseudomonas aeruginosa
Contact List
Julia E. Bandow
contact affiliationApplied Microbiology, Faculty of Biology and Biotechnology, Ruhr University Bochum, 44780 Bochum, Germany
contact emailjulia.bandow@rub.de
lab head
Christoph Senges
contact affiliationRuhr University Bochum
contact emailchristoph.senges@rub.de
dataset submitter
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2021/03/PXD012622
PRIDE project URI
Repository Record List
[ + ]