{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067556/20203030_Nsco_DDA_PASF_BP_WT_B2_GA6_1_399.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067556/20203030_Nsco_DDA_PASF_BP_WT_B4_GB8_1_379.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067556/Maxquant_search.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067556/20203030_Nsco_DDA_PASF_BP_delta_tig_B4_GC4_1_387.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067556/20203030_Nsco_DDA_PASF_BP_delta_tig_B1_GA5_1_397.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067556/20203030_Nsco_DDA_PASF_BP_delta_tig_B2_GB2_1_367.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067556/20203030_Nsco_DDA_PASF_BP_delta_tig_B3_GB7_1_377.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067556/20203030_Nsco_DDA_PASF_BP_WT_B1_GA1_1_389.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067556/20203030_Nsco_DDA_PASF_BP_WT_B3_GB3_1_369.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["mitali.sarkar-tyson@uwa.edu.au"],"submitter":["Nichollas Scott"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Lfq","Burkholderia pseudomallei"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067556"],"sample_protocol":["Cells grown to stationary phase on Blood agar, were harvested in PBS, washed and then solubilised inlysed in lysis buffer (4% SDS, 10 mM dithiothreitol, 100 mM Tris, pH 8.5) by boiling for 10 minutes. Bicinchoninic acid protein assay was used to assess the protein content as per the manufacturer’s instructions and 1mg of protein acetone precipitated overnight in 80% ice-cold acetone at -20°C.. Acetone precipitated protein were collected and dried prior to being solubilized in 4% SDS, 100mM Tris pH8.5 by boiling for 10 min at 95 °C. 200g of each biological replicate prepared for digestion using Mini S-traps column (Protifi, USA) according to the manufacturer’s instructions. Briefly, samples were reduced with 10mM Dithiothreitol for 10 mins at 95°C and then alkylated with 40mM 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 400l of S-trap wash buffer. Samples were then digested with 2 g of Trypsin/Lys-C (Promega, 1:100 protease/protein ratio) in 100mM Tetraethylammonium bromide 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."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Prepared C18 purified peptides from each sample 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 and a PepMap C18 500-mm by 75-m analytical column (Thermo Fisher Scientific). Samples were concentrated onto the trap column at 5 l/min for 5 min with Buffer A (0.1% formic acid, 2% DMSO) and then infused into a timsTOF Pro (Bruker) at 300 nl/minute via the analytical columns using a Dionex Ultimate 3000 UPLCs (Thermo Fisher Scientific). 120-minute analytical runs were undertaken by altering the buffer composition from 2% Buffer B (0.1% formic acid, 77.9% acetonitrile, 2% DMSO) to 22% B over 95 min, then from 22% B to 40% B over 10 min, then from 40% B to 80% B over 5 min. The composition was held at 80% B for 5 min, and then dropped to 2% B over 2 min before being held at 2% B for another 8 min. The timsTOF Pro was operated in DDA PASEF mode using Compass Hystar 5.1.8.1 with a 1.1 sec cycle time. Identification and LFQ analysis were accomplished using MaxQuant (v1.6.17.0) against the B. pseudomallei strain K96243 proteomes (Uniprot accession: UP000000605). Samples were searched allowing oxidation on Methionine as a variable modification as well as Carbamidomethyl of cystine as a fixed modification. Both LFQ and “Match Between Run” options were enabled to allow comparison between samples. The resulting data files were processed using Perseus (v1.4.0.6) to compare the growth conditions using student t-tests as well as Pearson correlation analyses."],"omics_type":["Proteomics"],"labhead":["Dr Mitali Sarkar-Tyson"],"instrument_platform":[""],"labhead_affiliation":["Marshall Centre for Infectious Diseases Research and Training, School of Biomedical Sciences, University of Western Australia, Perth, Western Australia, Australia"],"submission_type":["PARTIAL"],"species":["Burkholderia Pseudomallei (strain K96243)"],"submitter_mail":["nichollas.scott@unimelb.edu.au"],"publication":["Not available"],"submitter_affiliation":["University of Melbourne"],"submitter_country":["Australia"],"additional_accession":[]},"is_claimable":false,"name":"Trigger Factor in Burkholderia pseudomallei is essential for key virulence determinants including host cell internalisation, cytotoxicity, motility and stress resistance.","description":"Melioidosis is a potentially fatal infection caused by Burkholderia pseudomallei, a bacterium that is intrinsically resistant to many commonly used antibiotics.  Therefore, the identification of new drug targets is essential for the development of new and effective therapies. This study demonstrates that the Trigger Factor protein, encoded by BPSL1402, is important for the establishment of B. pseudomallei infection and is involved in multiple facets of virulence including motility, cell cytotoxicity and resistance to stress. With reports of B. pseudomallei isolated from new regions and resistance to current treatment options, the significance of this research is the identification of a novel B. pseudomallei virulence factor that can be potentially exploited for the development of new therapeutics to treat this deadly 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