{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075197/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075197/proteins.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075197/CK.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075197/SirM.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["yfyao@sjtu.edu.cn"],"submitter":["Zuoqiang Wang"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":["Not available"],"submitter_keywords":["phagocytosis","methyltransferase","heme","tlr4","Macrophage; phagocytosis; methyltransferase; heme; tlr4","Macrophage"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075197"],"sample_protocol":["The IP sample was denatured in 2% SDS buffer containing 50 mM DTT for 20 min at room temperature (RT), followed by boiling at 100°C for 5 min. Proteins were alkylated in the dark for 1 h at RT with 200 mM iodoacetamide (IAA). Subsequently, five volumes of pre-cooled acetone were added, and proteins were precipitated overnight at -20°C. The protein pellet was resolubilized and digested with sequencing-grade modified trypsin (Promega) at an enzyme-to-protein ratio of 1:50 (w/w) overnight at 37°C. Tryptic peptides were collected by centrifugation at 14,000 g for 20 min at 20°C, acidified with 1% trifluoroacetic acid (TFA), and desalted using C18 Ziptips. Peptides were eluted with 0.1% TFA in 50-70% acetonitrile, lyophilized in a SpeedVac (ThermoSavant), and resuspended in 10 µL of 1% formic acid/5% acetonitrile. All mass spectrometric experiments were performed on a Thermo Fusion Lumos mass spectrometer coupled to an Easy-nLC 1200 system via an Easy Spray source (Thermo Fisher Scientific). Peptide mixtures were loaded onto a 15 cm × 75 µm i.d. column packed with C18 2-µm reversed-phase resins (PepMap RSLC) and separated over a 60 min linear gradient from 95% solvent A (0.1% formic acid/2% acetonitrile) to 28% solvent B (0.1% formic acid/80% acetonitrile) at a flow rate of 300 nL/min. The spray voltage was set to 2.1 kV, ion transfer capillary temperature to 275°C, and RF lens to 60%. The mass spectrometer was operated in positive ion mode and data-dependent acquisition (DDA) mode using Tune and Xcalibur 4.0.27.19. Full MS scans (m/z 350-1500) were acquired at a resolution of 60,000 (at m/z 400), followed by fragmentation of the twenty most abundant multiply charged ions (charge states 2-7; excluding singly charged and unassigned ions) with collision energy of 30%. Dynamic exclusion was enabled with default settings."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["All MS/MS spectra were searched against the UniProt Salmonella Proteome database (Salmonella Typhimurium 14028s, Proteome ID: UP000002695) using PEAKS 11.0 (Bioinformatics Solutions) for de novo sequencing and database searching. The precursor and fragment mass error tolerances were set to 10 ppm and 0.02 Da, respectively. Semi-trypsin was specified as the digestion enzyme, allowing up to two missed cleavages. Carbamidomethylation of cysteine was set as a fixed modification, while oxidation of methionine and acetylation of the N-terminus were set as variable modifications. Peptide-spectrum matches (PSMs) were filtered with a −10logP score ≥ 20, and proteins were filtered with a −10logP score ≥ 15 and at least one unique peptide, resulting in an estimated FDR of less than 1% at the PSM level. Proteins sharing significant peptide evidence were grouped into clusters."],"omics_type":["Proteomics"],"labhead":["Yu-Feng Yao"],"instrument_platform":[""],"labhead_affiliation":["Shanghai Institute of Immunology, Shanghai Jiao Tong University School of Medicine."],"submission_type":["PARTIAL"],"species":["Salmonella Typhimurium (strain Lt2 / Sgsc1412 / Atcc 700720)"],"submitter_mail":["wallylovemolly@126.com"],"publication":["Not available"],"submitter_affiliation":["Shanghai Jiao Tong University School of Medicine"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Salmonella-derived heme inhibits macrophage phagocytosis and promotes infection in mice","description":"Bacterial pathogens such as Salmonella enterica serovar Typhimurium can resist phagocytosis by macrophages. Here we explored the role of bacterial heme biosynthesis in phagocytosis resistance. Using transposon sequencing (Tn-seq) during Salmonella infection of macrophages, we identify a methyltransferase, SirM, that indirectly inhibits phagocytosis of bacteria. Mechanistically, sirM is activated upon interaction with macrophages and methylates HemL, a key enzyme in heme biosynthesis, resulting in upregulation of heme synthesis by Salmonella. Salmonella-derived heme inhibits Cdc42 activation in a Toll-like receptor 4 (TLR4)-dependent manner to inhibit phagocytosis. Moreover, sirM promotes macrophage death by increasing heme synthesis. Experiments in mouse models show that sirM is required for virulence and confers a competitive advantage over intestinal commensal bacteria during infection. We also found that sirM is distributed among enteric pathogens. Collectively, our findings show that bacterial heme promotes evasion of phagocyte responses and pathogenesis to confer an advantage in the 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