{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/intermediate_SDRF.sdrf.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/CIP2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/CIP3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/No_CIP1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/CIP1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/No_CIP3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/No_CIP2.raw"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/mzTab.mzTab"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/CIP3.index","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/CIP2.index","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/No_CIP1.index","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/No_CIP2.index","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/No_CIP3.index","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069601/CIP1.index"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["bart.devreese@ugent.be"],"submitter":["Bart Devreese"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Stenotrophomonas maltophilia","Antibiotic resistance","Fluoroquinolone"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069601"],"sample_protocol":["Overnight cultures of S. maltophilia 44/98 WT were back-diluted in 100 ml of fresh LB-Lennox to reach an OD600 of 0.2, following which they were allowed to grow for 2 hours to reach early exponential phase. A sub-MIC of ciprofloxacin was added to the treatment cultures, and all cultures were allowed to grow for a further 3 hours. Subsequently, cultures were centrifuged at 8000 x g for 10 minutes at 4°C to pellet cells. Cell pellets were washed with ice-cold phosphate-buffered saline (PBS) and resuspended in a lysis buffer (6 M urea, 2 M thiourea, 50 mM ammonium bicarbonate), to which a cOmpleteTM EDTA-free Protease Inhibitor Tablet (Roche) was added to prevent protein degradation. Cell suspensions were sonicated using the following parameters – 1 second on, 8 seconds off at an intensity of 10 % for 2 minutes. Cell debris was pelleted  by centrifugation at 16000 x g for 10 minutes at 4°C, and trichloroacetic acid was added to the supernatants to reach a final concentration of approximately 2 % (v/v) to precipitate proteins overnight. The following day, precipitated proteins were pelleted by ultracentrifugation and washed with ice-cold PBS. Proteins were dried in a SpeedVac vacuum concentrator and resuspended in 50 mM ammonium bicarbonate. Proteins were quantified in triplicate using a Coomassie Protein Assay Kit (Thermo Scientific) with bovine serum albumin (BSA) as a standard. Samples were stored at –20°C until required.10 μg of each sample was dried in a SpeedVac vacuum concentrator and resuspended in 50 mM ammonium bicarbonate to reach a total volume of 50 μl. Samples were heated at 80°C for 10 minutes, following which they were reduced using DTT (50 mM, 10 minutes at 60°C) and alkylated using IAA (150 mM, 20 minutes in the dark at room temperature). Sequencing-grade modified trypsin (Promega) was added in a 1:50 ratio, and samples were incubated overnight in a water bath maintained at 37°C to allow for complete trypsinisation. The following day, samples were acidified using formic acid to stop the action of trypsin, and samples were centrifuged to precipitate any insoluble substances. The digestion mixtures were passed through 0.22 μm filters and dried in a SpeedVac vacuum concentrator. Dried peptides were resuspended in 0.1 % trifluoroacetic acid in water/acetonitrile (98:2 v/v) (loading solvent), and half of each sample was injected on an UltiMate 3000 RSLCnano UPHLC system (Thermo Scientific) connected in-line to an LTQ Orbitrap Elite mass spectrometer (Thermo Scientific) equipped with a PST-pneu-Nimbus dual-column source (Phoenix S&T, Pennsylvania). Trapping was performed at 10 μl/min for 4 minutes in solvent A on a 20 mm trapping column made in-house, with a 100 μm internal diameter and 5 μm C18 Reprosil-HD beads (Dr. Maisch, Germany). The samples were loaded on a 200 cm micro pillar array column (µPACTM) with C18-endcapped functionality (PharmaFluidics, Belgium), mounted in the UltiMate 3000 column oven at 50°C. To ensure proper ionisation, a fused silica PicoTip® emitter with a 10 µm inner diameter (New Objective, Massachusetts) was connected to the µPAC™ outlet union with a grounded connection. Peptides were eluted using a non-linear gradient reaching 9 % of 0.1 % formic acid in water/acetonitrile (2:8 v/v) (solvent B) in 15 minutes, 33 % solvent B in 105 minutes, 55 % solvent B in 125 minutes, and 99 % solvent B in 135 minutes, with an initial flow rate of 750 nl/min that was subsequently decreased to 300 nl/min, followed by a 15-minute wash reaching 99 % solvent B and re-equilibration with 0.1 % formic acid in water (solvent A). The mass spectrometer was operated in data-dependent positive ionisation mode, set to automatically switch between MS and MS/MS acquisition for the 20 most abundant peaks for a given MS spectrum. Source voltage was set at 1.8 kV and capillary temperature was set at 275°C. Full-scan MS spectra (300–2000 m/z; AGC target of 3 x 106 ions, maximum ion injection time of 100 ms) were acquired in the Orbitrap with a precursor resolution of 60000 at 400 m/z. The 20 most intense ions that satisfied a defined set of selection criteria (AGC target 5 x 103 ions, maximum ion injection time of 20 ms, centroid spectrum data type, exclusion of unassigned and singly positive charged precursors, dynamic exclusion time of 20 s) were subsequently isolated in the linear ion trap and fragmented in the high pressure cell through collision-induced dissociation (CID). Collision energy was set to 35 V, and the polydimethylcyclosiloxane background ion at 445.120028 Da was used for internal calibration."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Data was processed using MaxQuant (version 2.4.4.0) and the integrated search engine Andromeda (Cox and Mann 2008). Identification of proteins was done by searching the raw data files against a database comprised of protein sequences identified from the genomic analyses performed earlier. Carbamidomethylation of cysteine and oxidation of methionine were selected as fixed or variable modifications respectively. Trypsin was selected as the proteolytic enzyme, and up to 2 missed cleavages were allowed. The intensities of the proteins were determined by summing up the intensities of razor and unique peptides, and these were normalised to obtain label-free quantification (LFQ) intensities. Missing values were replaced with low abundance measurements generated from the normal distribution. Statistical significance was assessed with Perseus (version 2.1.3.0) using a two-sample t-test (fold-change > 2, q-value < 0.05). Identified proteins were searched against the UniProt database to identify their orthologues in the genome of the type-strain K279a."],"omics_type":["Proteomics"],"labhead":["Bart Devreese"],"instrument_platform":[""],"labhead_affiliation":["Laboratory for Microbiology, Department of Biochemistry and Microbiology, Ghent University, Belgium"],"submission_type":["COMPLETE"],"species":["Stenotrophomonas Maltophilia"],"publication":["10.1128/JB.00158-26"],"submitter_mail":["bart.devreese@ugent.be"],"submitter_affiliation":["Department of Biochemistry and Microbiology, Ghent Univers"],"submitter_country":["Belgium"],"doi":["10.6019/PXD069601"],"additional_accession":[]},"is_claimable":false,"name":"Stenotrophomonas maltophilia ciprofloxacin response","description":"In this project, the impact of subinhibitory concentrations of the fluoroquinolone ciprofloxacin on the multiresistant bacterium Stenotrophomonas maltophilia (strain LMG 26824) has been investigated. A label free proteomics analysis was performed to analyse the proteome of cells incubated with ciprofloxacin compared to a control 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