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uisa Nieto Ramirez"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Antigen presentation","Co-immunoprecipitation","Endosomal trafficking","Mr1"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062277"],"tissue":["Epithelial Cell"],"sample_protocol":["BEAS-2B cells over-expressing MR1-GFP carrying different mutations were treated with the MR1-stabilizing ligand 6-formylpterin and lysed in 1% digitonin + protease inhibitor cocktail (Roche). MR1-GFP was immunoprecipitated with GFPTrap magnetic agarose coupled to an anti-GFP nanobody (Chromotek) from two cell lines over-expressing mutated MR1 (D4: WT-like V12S mutation; D6: one 6-basepair insertion and one 24-basepair deletion). Agarose-bound proteins were boiled in NuPAGE LDS loading buffer(4X) mixed with 50 mM DTT (both Invitrogen) before briefly running on a 4-20% polyacrylamide gel (Bio-Rad). Gels were stained with Coomassie, and the gel sections containing the proteins were cut into small pieces for in-gel digestion. Briefly, the gel pieces were destained using 60% acetonitrile in 0.2 M ammonium bicarbonate, then dried. The dried gel pieces were mixed with 18 µL of trypsin (at a concentration of 0.083 µg/µL in 0.2 M ammonium bicarbonate) and incubated for 17 hours at 37°C. Extracted peptides were diluted in 3% acetonitrile and 0.1% formic acid in water. All reagents used were of LC/MS grade. The experiment was conducted in three different days, with four injections on day 1 and three injections on days 2 and 3 for each sample. Peptide concentration was quantified using a nanodrop, and 0.25 µg of peptides per sample were loaded onto a trap cartridge (PepMap™ Neo 5 μm C18 300 μm X 5 mm, Thermo FisherScientific) and separated on an analytical column (10 cm × 75 µm, C18, 1.9 µm, BrukerDaltonics). The gradient was generated using nanoElute liquid chromatography (LC) system (Bruker Daltonics, Bremen, Germany) with solvent A (0.1% formic acid in water) and solvent B (0.1% formic acid in acetonitrile). The gradient was 5%–30% of solvent B in 17.8 min, 30%–95% solvent B in 0.5 min, maintaining at 95% solvent B for 2.4 min at a flow rate of 500 nL.min−1. The LC system was connected to a TIMS TOF Flex mass spectrometer (Bruker Daltonics) via a CaptiveSpray nano-electrospray source, with a capillary voltage of 1600 V, dry gas at 3.0 L/min, and dry temperature at 200 °C. For the quantitative analysis, data independent acquisition (DIA)-PASEF mode was used, with a windows scheme of 7 MS/MS ramps with 19 mass steps per cycle, and a cycle time of 0.65s. Mass overlap and mass width were set to 1.0 Da and of 50 Da respectively, covering a mass-over-charge (m/z) range from 307.8 to 1,239.8. A linear collision energy ramp was used for peptide fragmentation: from 20-59, with an ion mobility range from 0.6 to 1.6 Vs/cm2. For all experiments, we calibrated both m/z and ion mobility dimension linearly using three compounds of the following m/z and ion mobility (m/z, 1/K0) values: 622.029, 0.99915 Vs/cm2; 922.0098, 1.1986 Vs/cm2; and 1221.9906, 1.3934 Vs/cm2. For the spectral library generation, three samples per strain were injected once for Data Dependent Acquisition (DDA)–Parallel accumulation Serial Fragmentation (PASEF) mode. Ramp time was set to 75 ms, resulting in an accumulation time of 75 ms and total cycle time of 0.57s. DDA analysis with 6 PASEF scans covered a mass range from 100 m/z to 1700 m/z."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The raw data files were analyzed using FragPipe version 22.0 to obtain protein identifications and their respective label-free quantification (LFQ) values. FragPipe version 22.0 contained the MSFragger version 4.1 database search tool for peptide identification, , MSBooster version 1.2.31 for rescoring using deep learning predictions, diaTracer version 1.1.5 for spectrum deconvolution of our DIA-PASEF data, EasyPQP version 0.1.50 for library generation, and the built-in DIANN version 1.8.2 Beta 8 for protein quantification, among other embedded validation tools. Peptide sequences were searched against the Homo sapiens proteome (UP000005640) retrieved from UniProt on 06/18/2024. Decoy and contaminant protein sequences were added to the human proteome FASTA file. For the MSFragger search, precursor tolerance was set to (-20) to 20 ppm and fragment tolerance was set to 20 ppm, with mass calibration and parameter optimization enabled. Isotope error was set to 0/1/2. One missed cleavage was allowed with trypsin digestion, along with the following variable modifications: oxidation of methionine (+15.9949) and acetylation of protein N-terminal (+42.0106). Additional settings included the top 150 most intense peaks and a minimum of 15 fragment peaks to search for a spectrum. Peptide spectral match (PSM) validation, protein interference, and false discovery rate (FDR) filtering were performed using Percolator, ProteinProphet, and Philosopher, respectively, to retain only the highest-scoring peptide matches for protein identification validation. A spectral library was generated using DDA data from the same samples run on the same instrument and using the same LC separation method. The default EasyPQP setup was used for spectral library generation, allowing a maximum unimod mass difference of 0.02 units and a maximum mass discrepancy of 15 PPM. Only b and y fragment ions were selected for peptide identification, with no retention time correction applied. The peptide ions in the spectral library were filtered with a 1% global peptide and protein FDR. The spectral library was then used to extract and quantify precursors, peptides, and proteins from the DIA data using DIA-NN. Normalized MaxLFQ intensity was used for protein quantification. Statistical analysis was performed using FragPipe-Analyst that has an in-house generated R script based on the ProteinGroup.txt file of DIA-NN. First, contaminant proteins, reverse sequences and proteins identified “only by site” were filtered out. In addition, proteins that have been only identified by a single peptide and proteins not identified/quantified consistently in same condition have been removed as well. The LFQ data was converted to log2 scale, samples were grouped by conditions and missing values were imputed using the ‘Missing not At Random’ (MNAR) method, which uses random draws from a left-shifted Gaussian distribution of 1.8 StDev (standard deviation) apart with a width of 0.3. Protein-wise linear models combined with empirical Bayes statistics were used for the differential expression analyses. The limma package from R Bioconductor was used to generate a list of differentially expressed proteins for each pair-wise comparison. A cutoff of the adjusted p-value of 0.01 (Benjamini-Hochberg method) along with a |log2 fold change| of 1 has been applied to determine significantly regulated proteins in each pairwise comparison."],"omics_type":["Proteomics"],"labhead":["Karen Dobos"],"instrument_platform":[""],"labhead_affiliation":["Professor, Microbiology, Immunology, and Pathology Colorado State University Co-Director, Mycobacteria Research Laboratories Scientific Director, Rocky Mountain Regional Biocontainment Laboratory"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["41759736 Kulicke CA, Lemon C, Krawic JR, Nieto Ramirez LM, Kim SJ, Narayanan G, Tafesse FG, Hildebrand WH, Dobos KM, Lewinsohn DM. Mutations outside the MR1 antigen binding groove differentially inhibit presentation of exogenous antigens. J Biol Chem. 2026 302(4):111317 10.1016/j.jbc.2026.111317"],"submitter_mail":["luisam@colostate.edu"],"submitter_affiliation":["Colorado State University"],"submitter_country":["United States"],"pubmed_abstract":["The antigen presenting molecule major histocompatibility complex class I-related protein 1 (MR1) binds small molecule metabolites derived from the microbial riboflavin biosynthetic pathway and presents them at the cell surface for surveillance by MR1-restricted mucosal-associated invariant T cells (MAIT cells). MR1 ligands can originate in the extracellular space or in endosomal compartments that contain microbial pathogens. Distinct, complementary antigen processing and presentation pathways enable MR1 to survey diverse intracellular locations and present both exogenous and intracellular antigens. Here, we generated a panel of BEAS-2B MR1 KO cells reconstituted with MR1 proteins mutated at amino acids 9 to 16. The overexpressed mutated MR1 molecules differentially translocated to the cell surface in response to 6-formylpterin and differed in their ability to present mycobacterial antigens to MAIT cell clones. While they barely presented Mycobacterium smegmatis supernatant and other exogenous MAIT cell antigens, their ability to present antigens derived from mycobacterial infection and a 5-amino-6-D-ribitylaminouracil prodrug that requires endosomal processing remained largely intact. Protein coimmunoprecipitation and mass spectrometry-based proteomic analysis showed that mutated MR1 differentially associated with calnexin and β<sub>2</sub>-microglobulin (B2M). Knock down of B2M in cells overexpressing wildtype MR1 phenocopied the loss of exogenous antigen presentation but did not impact presentation of intracellular antigens. Thus, the MR1-mediated presentation of exogenous antigen appears to be limited by binding to B2M whereas a lower sensitivity to B2M deficiency suggests that MAIT cell activation via the endosomal antigen presentation pathway may be limited by the availability of MR1 itself."],"pubmed_title":["Mutations outside the MR1 antigen binding groove differentially inhibit presentation of exogenous antigens."],"pubmed_authors":["Kulicke Corinna A CA, Lemon Chance C, Krawic Jason R JR, Nieto Ramirez Luisa Maria LM, Kim Se-Jin SJ, Narayanan Gitanjali G, Tafesse Fikadu G FG, Hildebrand William H WH, Dobos Karen M KM, Lewinsohn David M DM"],"additional_accession":[]},"is_claimable":false,"name":"Co-immunoprecipitation and proteomic analysis of Major Histocompatibility Complex Class I-related (MR1) mutants","description":"Identification of cellular proteins mediating presentation of bacterial antigens by the MHC I-related protein MR1. MR1 mutant proteins that differ in their capacity to present antigens from different sources were immunoprecipitated and their interacting proteins were compared to identify candidate proteins involved in the different antigen presentation pathways.","dates":{"publication":"2026-04-06","submission":"2025-03-27"},"accession":"PXD062277","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:46429","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:2736291","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:2767846","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:468822","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:342808","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:709964","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:156974","NEWT:3714","NCBITaxon:37162","NEWT:3715","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:9014","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:29022","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:1883426","NEWT:8165","NEWT:96794","NEWT:10401","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:215451","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:329032","NEWT:56636","NEWT:2499525","NEWT:55307","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:141469","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:1578","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:291146","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:911022","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:717989","NEWT:33952","NEWT:1255232","NEWT:11723","NEWT:445","NEWT:153009","NEWT:1004879","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:156981","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:2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