{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_RSA04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_RSA06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_RSA08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_Rha03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_RSA02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_Rha07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_Rha05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_Rha02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_RSA03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_RSA01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_RSA07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_Rha04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_Rha06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_Rha08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_RSA05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/250224_HT-10318_Rha01.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/Burkholderia_J2315_rha_TMP_cmyR.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/2024-09-27-decoys-contam-Burkholderia_J2315_rha_TMP_cmyR.fasta.fas"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/MSfragger-DIA.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070275/DIA_script.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["nichollas.scott@unimelb.edu.au"],"submitter":["Nichollas Scott"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Burkholderia","Cumate"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070275"],"sample_protocol":["Proteomic sample preparation and LC-MS analysis: B. cenocepacia cultures for proteomic analysis were incubated overnight with or without inducers (Cumate, Rhamnose) induction, under shaking conditions at 180 rpm. Cultures were adjusted to an OD₆₀₀ of 1.0, harvested by centrifugation at 10,000 × g for 10 minutes at 4 °C, washed three times with ice-cold PBS, and snap-frozen at −80 °C until further processing. Frozen whole-cell samples were solubilised in 4% SDS, 100mM Tris pH 8.5 by boiling for 10 min at 95 °C then protein concentrations assessed by bicinchoninic acid protein assays (Thermo Fisher Scientific). 100μg of each biological replicate/ sample was prepared for digestion using S-traps (Protifi, USA) mini columns according to the manufacturer’s instructions. Briefly, samples were reduced with 10mM Dithiothreitol for 20 mins at 95°C and then alkylated with 50mM Iodoacetamide in the dark for 1 hour. Samples were acidified to 1.2% phosphoric acid and diluted with seven volumes of S-trap wash buffer (90% methanol, 100mM Tetraethylammonium bromide pH 7.1) before being loaded onto S-traps and washed 3 times with S-trap wash buffer. Samples were then digested with 2 μg of SoluTrypsin (Sigma) overnight at 37°C before being collected by centrifugation with washes of 100mM Tetraethylammonium bromide, followed by 0.2% formic acid followed by 0.2% formic acid / 50% acetonitrile. Samples were dried down and further cleaned up using C18 Stage tips to ensure the removal of any particulate matter.  Reverse phase Liquid chromatography–mass spectrometry: C18 enriched proteome samples were re-suspended in Buffer A* (2% acetonitrile, 0.01% trifluoroacetic acid) and separated using a two-column chromatography setup composed of a PepMap100 C18 20-mm by 75-m trap (Thermo Fisher Scientific) and a PepMap C18 500-mm by 75-m analytical column (Thermo Fisher Scientific) using a Dionex Ultimate 3000 UPLC (Thermo Fisher Scientific). Samples were concentrated onto the trap column at 5 l/min for 6 min with Buffer A (0.1% formic acid, 2% DMSO) and then infused into an Orbitrap Eclipse™ (Thermo Fisher Scientific) at 300 nl/minute via the analytical columns. Peptides were separated by altering the buffer composition from 3% Buffer B (0.1% formic acid, 77.9% acetonitrile, 2% DMSO) to 28% B over 70 minutes, then from 23% B to 40% B over 4 minutes and then from 40% B to 80% B over 3 minutes. The composition was held at 80% B for 2 minutes before being returned to 3% B for 10 minutes. The Orbitrap Eclipse was operated in a data-independent mode automatically switching between the acquisition of a single Orbitrap MS1 event (120k resolution, AGC 1*106, 350-1400 m/z) and 50 MS2 scans (NCE 30%, 30k resolution, AGC 1*106, 200-2000 m/z and a maximal injection time of 55 ms) of a width of 13.7 m/z collected over the mass range of 361 to 1033 m/z."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["DIA-based proteomic analysis: DIA data was searched with MSFragger (versions 22.0) using the “DIA_SpecLib_Quant” workflow utilizing DIA-NN. Samples were searched with a Tryptic specificity, allowing a maximum of two missed cleavage events and Carbamidomethyl set as a fixed modification of Cysteine while oxidation of Methionine allowed as a variable modification. A maximum mass precursor tolerance of 20 ppm was allowed at both the MS1 and MS2 levels. Samples were searched against the B. cenocepacia reference proteome J2315 (Uniprot accession: UP000001035, 6,993 proteins, downloaded July 24th 2020) 93 supplemented with the proteins RhaS (HTH-type transcriptional activator RhaS, P09377), RhaR (HTH-type transcriptional activator RhaR, P09378), TmpR (Dihydrofolate reductase resistance marker, P00384) and CymR (HTH-type transcriptional regulator CymR, O33453). DIA-NN-based quantitation used for statistical analysis of protein abundances and analysed within Perseus 95. Missing values were imputed based on the total observed protein intensities with a range of 0.3 σ and a downshift of 2.5 σ with biological replicates grouped together to allow comparison by student t-tests. Proteins were considered altered if they sastisified both p-value and fold change alterations as defined by the function y = c/(x - x0) where c = curvature and  x0 = minimum fold change with were x0 = 1 and c = 4. Data visualization was undertaken using ggplot2 96 in R."],"omics_type":["Proteomics"],"labhead":["Nichollas E. Scott"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Microbiology and Immunology, University of Melbourne, Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, Australia"],"species":["Burkholderia Cenocepacia K56-2valvano"],"publication":["Not available"],"submitter_mail":["nichollas.scott@unimelb.edu.au"],"submitter_affiliation":["University of Melbourne"],"submitter_country":["Australia"],"additional_accession":[]},"is_claimable":false,"name":"Generation of an optimized Cumate circuit toolkit for tunable protein expression during in vitro and in vivo studies of Burkholderia cenocepacia: DIA experiment cumate vs Rhamnose","description":"Inducible gene expression systems are pivotal for dissecting bacterial physiology and virulence mechanisms. Across the Burkholderia genera, a limited range of inducible systems currently exist that show minimal impacts on the proteome and allow tight regulation. In this study, we engineer a set of cumate-inducible vectors for use in Burkholderia cenocepacia that offer minimal basal expression and the ability to control B. cenocepacia gene expression within Eukaryotic cells. Through mutagenesis-based studies of cumate circuits and the cumate regulator (CymR), we generate an optimized cumate circuit (PCymRC/CymRGV) which allows the tight and tunable control of protein expression within B. cenocepacia as assessed by fluorescent and protein O-linked glycosylation analysis. Using comparative proteomics, we demonstrate cumate induction leads to both reduced and orthogonal effects on B. cenocepacia compared to widely used rhamnose based induction systems. Leveraging the cell permeability of cumate and the generation of a CTX-based chromosomal integration vector, we show inducible control of protein expression is achievable during intracellular replication of B. cenocepacia. Finally, using the ability to control intracellular expression, we demonstrate the requirement of O-linked protein glycosylation for optimal B. cenocepacia intracellular replication. Combined, this work demonstrates that cumate inducible systems allows precise and tuneable gene expression in Burkholderia even within a host-pathogen 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