{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/report-lib.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/report.pg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/report.pr_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/report.gg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/report.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/report.stats.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/report.log.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/checksum.txt"],"Pdf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/report.pdf"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/FASTA_Protein_ContamPrefix_Hao_Lab.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/Salmonella_typhimurium_strain_SL1344_4659_20230914.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/Human_SwissProt_42437_20230914.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_30min_UC_highsens_2_S4-B2_1_8827.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_4h_UC_highsens_4_S4-B10_1_8836.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_4h_UC_highsens_3_S4-B9_1_8835.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_30min_UC_highsens_4_S4-B4_1_8829.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_30min_UC_highsens_5_S4-B5_1_8830.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/report.parquet","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_4h_UC_highsens_6_S4-B12_1_8838.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_4h_UC_highsens_2_S4-B8_1_8834.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_4h_UC_highsens_5_S4-B11_1_8837.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_30min_UC_highsens_1_S4-B1_1_8826.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_30min_UC_highsens_3_S4-B3_1_8828.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_4h_UC_highsens_1_S4-B7_1_8833.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD076727/20241002_RC_STM_WT_30min_UC_highsens_6_S4-B6_1_8831.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["matthias.trost@manchester.ac.uk"],"submitter":["Matthias Trost"],"technology_type":["Mass Spectrometry","diaPASEF","Data-independent acquisition","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Salmonella","Bacteria","Phagosome"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD076727"],"tissue":["Cell Culture","Macrophage"],"sample_protocol":["After sorting, the samples were centrifuged at 15,000 rpm for 15 min at 4°C, resuspended in PBS supplemented with protease inhibitors, transferred to low protein binding microcentrifuge tubes, and dried in a vacuum concentrator. Next, the samples were resuspended in a 50 μL lysis buffer supplemented with protease inhibitors. To prepare the samples for mass spectrometry, S-Trap micro columns (Protifi) were used according to the manufacturer's recommended protocol for high recovery. Proteins were reduced with 20 mM tris(2-carboxyethyl)phosphine at 37ºC for 30 min and alkylated with 20 mM iodoacetamide in the dark for 30 min. The proteins were then acidified with 5 μL 55 % phosphoric acid and 330 μL S-Trap binding buffer. Two micrograms of Sequencing Grade Modified Trypsin (Promega) were added to the acidified samples before being transferred into the S-Trap column. The columns were washed five times with 150 μL S-Trap binding buffer before incubating them with 0.5 μg of Sequencing Grade Modified Trypsin in 25 μl of 50 mM TEAB, pH 8 for 2 h at 47°C. Finally, the samples were sequentially eluted in 40 μl 50 mM TEAB, pH 8, 40 μl 0.2 % formic acid and 35 μl 50 % acetonitrile with 0.2 % formic acid. The eluted peptides were dried in a vacuum concentrator and stored in -80°C until further use. Liquid chromatography (LC) was performed using an Evosep One system with a 15 cm Aurora Elite C18 column with integrated captive spray emitter (IonOpticks), at 50 °C. Buffer A was 0.1 % formic acid in HPLC water, buffer B was 0.1 % formic acid in acetonitrile. Immediately prior to LC-MS, peptides were resuspended in 30 µl of buffer A and a volume of peptides equivalent to 20 % of the sample (100,000 events isolated during the FACS) was loaded onto the LC system-specific C18 EvoTips, according to manufacturer instructions, and subjected to the predefined Whisper100 or Whisper-Zoom 20 SPD protocol (where the gradient is 0-35 % buffer B, 100 nl/min or 200 nl/min, for 58 minutes, 20 samples per day were permitted, and the same LC method was used within experiments). The Evosep One was used in line with a timsToF-HT mass spectrometer (Bruker) operated in DIA-PASEF mode with high sensitivity on. Mass and IM ranges were 300-1200 m/z and 0.6-1.45 1/K0, DIA-PASEF was performed as previously using variable width IM-m/z windows without overlap, designed using py_diAID, and are provided (see data sharing section). TIMS ramp and accumulation times were 100 ms, total cycle time was ~1.8 seconds. Collision energy was applied in a linear fashion, where ion mobility = 0.6-1.6 1/K0, and collision energy = 20 - 59 eV."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw data files were searched using DIA-NN 1.9, using its in silico generated spectral library from the Homo sapiens (downloaded from Uniprot on the 14th of September 2023, containing 42437 entries) and Salmonella Typhimurium (downloaded from Uniprot on the 14th of September 2023 containing 4659 entries) or E. coli (downloaded from Uniprot on the 03rd of June 2021 containing 4340 entries) proteomes and a common contaminants list. Carbamidomethylation (C) was set as a fixed modification, and oxidation (M) to variable. Precursor masses from 300 to 1800 were included, with charge 1 to 4. Mass accuracy for MS1 and MS2 was set to 15, Match between runs was performed and normalisation set to ‘Global’. Trypsin specificity was set to one missed cleavages and a protein and PSM false discovery rate of 1%, respectively. The statistical analysis was performed using the R package Limma with a Q-value (adjusted p-value) threshold of adjusted p-value < 0.05."],"omics_type":["Proteomics"],"labhead":["Matthias Trost"],"instrument_platform":[""],"labhead_affiliation":["University of Manchester, Newcastle University"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)","Salmonella Enterica Subsp. Enterica Serovar Typhimurium Str. Sl1344"],"submitter_mail":["matthias.trost@ncl.ac.uk"],"publication":["Not available"],"submitter_affiliation":["Newcastle University"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Flow cytometry-based isolation and ultra-sensitive proteomics of Salmonella-containing phagosomes provides novel insights into pathogen interactions with host cells","description":"Bacterial infections can be life-threatening to both humans and animals, an affliction bearing a tremendous economic burden-as testified by the incidence of antimicrobial resistance. During infection, innate immune cells from the host present the first line of defense as invading pathogens are engulfed into specialized de novo organelles called phagosomes. These phagosomes mature into lysosomes, establishing a hostile environment in which the pathogen is effectively neutralized and degraded. Most intracellular pathogens actively manipulate the maturation of phagosomes as a means to support their survival and replication within immune cells like macrophages, such as Salmonella enterica spp. Although this interaction is of paramount importance, the details about its molecular level are not well understood because of a number of technical difficulties in the isolation of pure bacteria-containing phagosomes and their highly complex network. Furthermore, even within one macrophage, phagosomes exhibit extreme heterogeneity, which pathogens exploit for their own benefit. In the face of these challenges, we have developed a novel approach using antibody-free fluorescence-activated cell sorting to purify intact bacteria-containing phagosomes. Subsequent ultrasensitive mass spectrometry-based proteomics thus allow the identification of host and bacterial proteins present on these phagosomes at nano-gram levels. We applied this strategy for the purification of Salmonella-containing vacuoles (SCVs) from infected human THP-1 macrophages highlighting an tug-of-war kind of host-pathogen battle. Our results show reproducibility and robustness of our strategy and confirm literature while revealing new information on host proteins playing a role in magnesium transport across the SCV membrane at various steps of infection. Moreover, we observed changes in the host and bacterial proteins, in terms of stress, innate immunity, and virulence responses, are induced through what the Salmonella PhoP/Q system, one of the most basic influences on the human phagosome proteome in a time-dependent manner, has 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