{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079152/psm.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079152/ion.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079152/protein.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079152/peptide.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079152/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079152/OR3_2025_07_19_JS25_005_flag_R.raw"],"Pepxml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079152/OR3_2025_07_19_JS25_005_flag_R.pepXML"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["mhornef@ukaachen.de"],"submitter":["Marlene Birk"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":["Salmonella","Lc-msms","Sopb interactors","Tmt"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079152"],"tissue":["Cell Culture"],"sample_protocol":["Polarized, confluent m-ICcl2 cells were infected with S. Typhimurium expressing 3×FLAG-SopB or an untagged wild-type control (3 biological replicates each). Following infection, cells were lysed and SopB-associated protein complexes were enriched by anti-FLAG affinity purification. Bound proteins were eluted with FLAG peptide, reduced, alkylated, treated with Benzonase, and processed using an SP3-based sample preparation workflow. Proteins were digested with Trypsin/LysC and peptides were labeled with 6-plex TMT. Samples were pooled, desalted, and analyzed by nanoLC-MS/MS on an Orbitrap Exploris 480 coupled to an UltiMate 3000 RSLCnano system. Raw data were processed with MSFragger (v3.8) against combined Mus musculus and S. Typhimurium 14028S UniProt databases, including contaminant and decoy sequences."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw MS files were converted to mzML and analyzed using the MSFragger TMT workflow (v3.8) in FragPipe (v20.0). Spectra were searched against combined Mus musculus and S. Typhimurium 14028S UniProt proteomes, including contaminant and decoy sequences. Searches used trypsin specificity with up to two missed cleavages; carbamidomethylation and TMT labeling were set as fixed modifications, while methionine oxidation, protein N-terminal acetylation, and peptide N-terminal TMT labeling were treated as variable modifications. Peptide-spectrum matches, peptides, and proteins were filtered to a 1% false discovery rate. Proteins identified by at least one unique peptide were retained. Quantitative data were normalized using VSN and analyzed in R with limma. Differential protein abundance was assessed using linear models with empirical Bayes moderation, and p-values were adjusted for multiple testing using the Benjamini–Hochberg false discovery rate method."],"omics_type":["Proteomics"],"labhead":["Prof. Dr. Mathias Walter Hornef"],"instrument_platform":[""],"labhead_affiliation":["Institute for Medical Microbiology   Universitätsklinikum der RWTH Aachen, Germany"],"submission_type":["PARTIAL"],"species":["Salmonella Typhimurium (strain 14028s / Sgsc 2262)","Mus Musculus (mouse)"],"publication":["42409845 Diab N,Yong CH,Stange EL,Birk MS,Schmitz MA,Düsterhöft S,Pes J,Ferle KN,Karkossa I,Schubert K,Deiwick J,Vucur M,Luedde T,Torow N,Ludwig A,Dupont A,Selkrig J,von Bergen M,Hensel M,Zhang K,Hornef MW Salmonella SopB suppresses post-transcriptionally regulated cytokine release to reduce early tissue inflammation and delay disease progression. Nat Commun. 2026 Jul 6 17(1) 10.1038/s41467-026-74942-9"],"submitter_mail":["mbirk@ukaachen.de"],"submitter_affiliation":["University Hospital Aachen"],"submitter_country":["Germany"],"pubmed_abstract":["Salmonella enterica subsp. enterica serovar Typhimurium (S. Typhimurium) manipulates cellular processes through the translocation of effector molecules into the host cell cytosol. Using a recently established neonatal S. Typhimurium infection model, we provide functional insights into how Salmonella outer protein B (SopB) suppresses early mucosal tissue inflammation and prolongs host survival. Mechanistically, SopB prevents a disintegrin and metalloprotease 17 (ADAM17) activation, plasma membrane translocation and the release of membrane-bound TNFα from enterocytes and reduces epithelial secretion of IL-18 via mTOR-controlled secretory autophagy. This abolishes the early epithelial transcriptional response and reduces immune cell recruitment and programmed cell death-mediated mucosal barrier disruption delaying disease progression. The immunosuppressive effect of SopB is independent of the C-terminally encoded phosphatidylinositol phosphatase and phosphotransferase activity but requires an intact N-terminal domain. Also, it is restricted to the neonatal mouse model characterised by Salmonella pathogenicity island (SPI)1 type 3 secretion system (T3SS)-dependent enterocyte invasion-driven mucosal translocation. Thus, here we demonstrate that SopB suppresses the early, post-transcriptional regulation of epithelial cytokine release in an inositol phosphatase-independent manner likely promoting pathogen transmission."],"pubmed_title":["Salmonella SopB suppresses post-transcriptionally regulated cytokine release to reduce early tissue inflammation and delay disease progression."],"pubmed_authors":["Diab Nour N, Yong Chiun Huei CH, Stange Eva-Lena EL, Birk Marlène S MS, Schmitz Matthias A MA, Düsterhöft Stefan S, Pes Jonas J, Ferle Kira Noemi KN, Karkossa Isabel I, Schubert Kristin K, Deiwick Jörg J, Vucur Mihael M, Luedde Tom T, Torow Natalia N, Ludwig Andreas A, Dupont Aline A, Selkrig Joel J, von Bergen Martin M, Hensel Michael M, Zhang Kaiyi K, Hornef Mathias W MW"],"additional_accession":[]},"is_claimable":false,"name":"Salmonella SopB suppresses post-transcriptionally regulated cytokine release to reduce early tissue inflammation and delay disease progression","description":"Salmonella enterica subsp. enterica serovar Typhimurium (S. Typhimurium) manipulates cellular processes through the translocation of effector molecules into the host cell cytosol. Using a recently established neonatal S. Typhimurium infection model, we provide functional insights into how Salmonella outer protein B (SopB) suppresses early mucosal tissue inflammation and prolongs host survival. Mechanistically, SopB prevents a disintegrin and  metalloprotease 17 (ADAM17) activation, plasma membrane translocation and the release of membrane-bound TNFa from enterocytes and reduces epithelial secretion of IL-18 via mTOR controlled secretory autophagy. This abolishes the early epithelial transcriptional response and reduces immune cell recruitment and programmed cell death-mediated mucosal barrier disruption delaying disease progression. The immunosuppressive effect of SopB is independent of the C-terminally encoded phosphatidylinositol phosphatase and phosphotransferase activity but requires an intact N-terminal domain. Thus, here we demonstrate that SopB suppresses the early, post-transcriptional regulation of epithelial cytokine release in an inositol phosphatase independent manner likely promoting pathogen 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