{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/sdrf.tsv"],"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/MBI_24932_all_groups_3vv_in_each_group_protein_report.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_12-2_21092025_9-24-2025_6467.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_0-2_21092025_9-24-2025_6463.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_24-4_21092025_9-23-2025_6453.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_24-1_21092025_9-23-2025_6454.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_24-C1_21092025_9-23-2025_6458.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_24-C2_21092025_9-23-2025_6455.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_24-3_21092025_9-23-2025_6456.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_2-1_21092025_9-24-2025_6468.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_0-4_21092025_9-24-2025_6472.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_12-1_21092025_9-24-2025_6466.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_0-1_21092025_9-24-2025_6462.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_24-2_21092025_9-23-2025_6459.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_2-2_21092025_9-24-2025_6461.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_2-4_21092025_9-24-2025_6465.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_12-3_21092025_9-24-2025_6464.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_24-C4_21092025_9-23-2025_6460.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_12-4_21092025_9-24-2025_6471.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_2-3_21092025_9-24-2025_6470.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_0-3_21092025_9-24-2025_6469.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075756/TTU_MB_24932_24-C3_21092025_9-23-2025_6457.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["moshe.biton@weizmann.ac.il"],"submitter":["Vladyslav Holiar"],"technology_type":["Mass Spectrometry","Top-down proteomics","Data-independent acquisition"],"disease":["Bacterial Infectious Disease"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075756"],"tissue":["Paneth Cell Of Epithelium Of Small Intestine","Small Intestine"],"sample_protocol":["Paneth cells (EpCAM+ CD24+ SSC-high) were FACS sorted and infected as described above. At different timepoints, Paneth cells were FACS sorted directly into 0.2% n-dodecyl β-D-maltoside (DDM) 150mM NaCl. The lysates were reduced with 6.25 mM dithiothreitol for 30 min followed by alkylation with 12.5 mM iodoacetamide in the dark for additional 30 min. Samples were then digested with 30ng of trypsin for 4 h at 37 °C. The digested peptides were acidified with 0.1% TFA. Samples were then vacuum-dried, resuspended in 0.1% TFA and kept at −80°C until analysis. Liquid chromatography Each sample was loaded using split-less nano-Ultra Performance Liquid Chromatography (nanoElute2, Bruker, Germany). The mobile phase was: A) H2O + 0.1% formic acid and B) acetonitrile + 0.1% formic acid. The peptides were separated using a trap Pepmap Neo C18 column (300μm ID x 5mm, Thermo scientific) and an Aurora column (75μm ID x 25cm, IonOpticks) at 0.3 µL/min. Peptides were eluted from the column into the mass spectrometer using the following gradient: 2% to 35%B in 30 min, 35% to 95%B in 30 sec, maintained at 95% for 3 min and then back to initial conditions. Mass Spectrometry The nanoUPLC was coupled online through a 10um ZDV emitter to a timsTOF Ultra mass spectrometer (Bruker Daltonics, Germany). Data was acquired in parallel accumulation–serial fragmentation combined with data independent acquisition (DIA-PASEF) mode103. For ion mobility 1/K0 range was set to 0.70-1.30 V/cm2, ramp time of 166 msec and estimated cycle time of 1.20 sec. 27 windows of 25 Da with 1 Da overlap were set over a range of 335.3-1011.3 Da."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw data was processed with DIA-NN v.2.2.0104. The data was searched in library-free mode against the M. musculus and S. Typhimurium Uniprot proteome databases appended with common lab protein contaminants and the following modifications: Carbamidomethylation of C as a fixed modification and oxidation of M and protein N-terminal acetylation as variable ones. Quantification was performed using the QuantUMS (high precision) algorithm. The Label-Free Quantification intensities were extracted and used for further calculations using Perseus v1.6.2.3105. Those intensities were log transformed and only proteins that had at least 3 valid values in at least one experimental group were kept. The remaining missing values were imputed (width=0.3 and down shift=1.8). A student’s t-test was performed to identify the proteins that are differentially expressed."],"omics_type":["Proteomics"],"labhead":["Moshe Biton"],"instrument_platform":[""],"labhead_affiliation":["Principal Investigator | The Ernst and Kaethe Ascher Career Development Chair | The Department of Immunology and Regenerative Biology | Weizmann-UK Building, Room 17 | Weizmann Institute of Science | Rehovot 76100, ISRAEL | Tel:  +972-8-934-4937"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["vlad.goliar@gmail.com"],"publication":["Not available"],"submitter_affiliation":["Weizmann Institute of Science"],"submitter_country":["Israel"],"additional_accession":[]},"is_claimable":false,"name":"An inflammasome-driven differentiation program in intestinal stem cells protects against Salmonella infection","description":"Intestinal stem cells (ISCs) are essential for sustaining epithelial renewal and barrier integrity, yet their role in orchestrating defense against enteric pathogens remains unclear. Here, we identify a stem cell–intrinsic immune mechanism whereby Lgr5⁺ ISCs detect intracellular Salmonella enterica and activate an inflammasome-dependent differentiation program. Using fluorescent-labeled Salmonella enterica, single-cell transcriptomics, fate mapping, organoid models, and genetic perturbations, we show that invaded ISCs undergo rapid reprogramming toward antimicrobial peptide-enriched Paneth cells via ASC (Pycard)-mediated inflammasome signaling. This fate switch enhances epithelial antimicrobial capacity and restricts pathogen persistence in the crypt. The response is Salmonella-specific and conserved in human intestinal organoids. Moreover, the invasion-associated transcriptional signature is enriched in ISCs from Crohn’s disease patients. Our findings reveal that ISCs act as active sensors of bacterial invasion and initiate epithelial remodeling through inflammasome signaling, highlighting stem cell plasticity as a frontline innate immune 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