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Following centrifugation at 18,000 × g for 10 minutes, the supernatant was collected for enrichment using an anti-MHC antibody (W6/32, BioLegend) conjugated to Affi-Gel 10 matrix (Bio-Rad; 2 mg of antibody per 100 µL of slurry per sample). Enrichment was performed by rotating the lysate with the resin at 4 °C for 4 hours, followed by transfer to a Bio-Spin column (Bio-Rad). Columns were sequentially washed with 3 × 1 mL of lysis buffer, wash buffer 1 (50 mM Tris-HCl pH 8.0, 150 mM NaCl), wash buffer 2 (50 mM Tris-HCl pH 8.0, 400 mM NaCl), and wash buffer 3 (50 mM Tris-HCl pH 8.0). MHC-bound peptides were eluted with 1 mL of 1% trifluoroacetic acid in water. Peptide samples were desalted using Sep-Pak C18 cartridges (Waters), dried by SpeedVac, and analyzed on an Orbitrap Eclipse Tribrid mass spectrometer coupled with a Vanquish Neo UHPLC system.  Peptides were loaded onto an EASY-Spray HPLC column (C18, 2 µm particle size, 75 µm inner diameter, 150 mm length) and eluted at a flow rate of 0.25 µL/min using the following gradient: 5% buffer B (80% acetonitrile with 0.1% formic acid) in buffer A (water with 0.1% formic acid) from 0 to 15 minutes; increasing to 35% buffer B from 15 to 155 minutes; and then from 35% to 100% buffer B from 155 to 180 minutes. The nano-LC electrospray ionization source was operated at 1.5 kV. Data were acquired in data-dependent acquisition (DDA) mode. High-field asymmetric waveform ion mobility spectrometry (FAIMS) was applied during analysis using three compensation voltages (-40, -50, and -60 V). The analysis began with an MS1 scan in the Orbitrap (resolution 60,000; m/z range 375-1600; RF lens at 60%; standard AGC target; automatic maximum injection time). For each FAIMS CV, precursor ions were isolated for MS2 using the quadrupole with a 0.7 m/z isolation window and fragmented via higher-energy collisional dissociation (HCD) in the ion trap (collision energy 27%; standard AGC target; maximum injection time 35 ms). RAW data were acquired using Xcalibur (version 4.5.445.18)."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["RAW files were processed using FragPipe (v23.1) with MSFragger for database searching. Spectra were searched using a nonspecific digestion mode, with peptide lengths restricted to 8-12 amino acids and a precursor mass range of 200-2,000 Da. The precursor mass tolerance was set to ±20 ppm and fragment mass tolerance to 0.6 Da. Mass calibration with parameter optimization was enabled. IA-mTz (+403.1856 Da), DBIA (+296.1848 Da), CA (+57.0215), DNCB (+166.0015), or cysteinylation (+119.0041 Da) were included as variable modifications on cysteine residues. No fixed modifications were specified. Search results were rescored using MSBooster with deep learning-based prediction of retention time and fragment ion spectra. Peptide-spectrum matches (PSMs) were validated using Percolator, and results were filtered to a 5% false discovery rate (FDR) at the PSM and peptide levels. Protein-level FDR filtering was not applied, consistent with immunopeptidomics workflows."],"omics_type":["Proteomics"],"labhead":["Xiaoyu Zhang"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Northwestern University, Department of Chemistry"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["zhang@northwestern.edu"],"submitter_affiliation":["Northwestern University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Expanding the repertoire of chemically induced covalent neoantigens","description":"The ubiquitin-proteasome system (UPS) generates peptide fragments that are displayed on class I major histocompatibility complex (MHC-I) molecules. Hapten-modified peptides, which are derived from proteins covalently modified by exogenous small molecules, have long been proposed as a mechanism for immune recognition. Building on this concept, recent studies have begun to harness this mechanism for therapeutic purposes, demonstrating that covalent small molecules can engage this pathway to drive the presentation of hapten-modified peptide fragments, or covalent neoantigens. Here, we report a platform to systematically investigate this process and harness covalent neoantigens for immune cell recruitment and activation. Using bioorthogonal cysteine-reactive probes, we demonstrate that covalently modified intracellular proteins can be processed and presented as covalent neoantigens in multiple cell lines. Immunopeptidomics confirmed the presence of probe-modified peptides within the MHC-I immunopeptidome. We further integrated a bioorthogonal strategy for immune cell engagement by pairing methyltetrazine (mTz)-tagged covalent neoantigens with trans-cyclooctene (TCO)-conjugated immune cell recruiters, leading to the activation of CD32- and CD3-expressing reporter immune cells. These findings indicate an expanded scope of covalent neoantigen formation and provide a generalizable strategy for immune targeting of covalent neoantigens.","dates":{"publication":"2026-07-08","submission":"2026-04-19"},"accession":"PXD077352","cross_references":{"TAXONOMY":["NEWT:3555","NEWT:71647","NEWT:330879","NEWT:35554","NEWT:32046","NEWT:544496","NEWT:2042546","NEWT:32049","NEWT:1392696","NEWT:259447","NEWT:295546","NEWT:45351","NEWT:445974","NEWT:43179","NEWT:180454","NEWT:5722","NCBITaxon:1280","NEWT:1129","NEWT:309807","NEWT:55153","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:43186","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:498019","NEWT:1351","NEWT:1438992","NEWT:1352","NEWT:2649997","NEWT:1147161","NEWT:638632","NEWT:263737","NEWT:224326","NEWT:1333499","NCBITaxon:79857","NEWT:1096976","NEWT:5702","NEWT:95648","NEWT:1589","NEWT:135622","NEWT:1349","NEWT:96731","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:44491","NEWT:641809","NEWT:27933","NEWT:556484","NEWT:317447","NEWT:4688","NEWT:7955","NEWT:7959","NEWT:2261","NEWT:31156","NEWT:3112","NEWT:79329","NEWT:4442","NEWT:192875","NEWT:1214915","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:108061","NEWT:60711","NEWT:1316931","NEWT:224308","NEWT:3347","NEWT:511145","NEWT:160621","NEWT:212790","NEWT:931281","NEWT:4432","NEWT:5762","NEWT:658457","NEWT:1310161","NEWT:77133","NEWT:295358","NEWT:145481","NCBITaxon:79824","NEWT:2246","NEWT:2652724","NEWT:1912919","NCBITaxon:4563","NEWT:5755","NEWT:44689","NEWT:44447","NEWT:752555","NEWT:498211","NEWT:5759","NEWT:1736231","NEWT:5518","NEWT:398007","NEWT:1392","NEWT:498217","NEWT:498216","NEWT:2242","NEWT:11320","NEWT:286","NEWT:391619","NEWT:246196","NEWT:287","NEWT:246197","NEWT:1367269","NEWT:633149","NEWT:10239","NEWT:44685","NEWT:161934","NEWT:4897","NEWT:1148","NEWT:5744","NEWT:5508","NEWT:3329","NEWT:5507","NEWT:410661","NEWT:55571","NEWT:35500","NEWT:1235816","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:4896","NEWT:1287689","NEWT:1390","NEWT:11557","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:294","NEWT:1773","NEWT:1182590","NEWT:3712","NEWT:82380","NEWT:3711","NEWT:935293","NEWT:375146","NEWT:2065263","NEWT:118698","NEWT:1616117","NEWT:263","NEWT:118696","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:408169","NEWT:44664","NEWT:47946","NEWT:3702","NEWT:243277","NEWT:1246791","NEWT:7067","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:33548","NEWT:274","NEWT:7070","NEWT:408172","NEWT:408170","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1436733","NEWT:460519","NEWT:1247411","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:9483","NEWT:333760","NEWT:1513458","NEWT:1233681","NCBITaxon:40559","NEWT:506599","NEWT:2853422","NEWT:84588","NEWT:1679718","NEWT:480","NEWT:65349","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:300852","NEWT:1502","NEWT:376686","NEWT:95486","NEWT:508771","NEWT:1883446","NEWT:253","NCBITaxon:2759","NEWT:1233435","NEWT:93061","NEWT:93062","NCBITaxon:4932","NEWT:109760","NEWT:943274","NEWT:644223","NEWT:235443","NEWT:108458","NEWT:5936","NEWT:272623","NEWT:272624","NEWT:320637","NEWT:983964","NEWT:118499","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:55529","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:476272","NEWT:3747","NEWT:195051","NEWT:3988","NEWT:1116234","NEWT:1255228","NEWT:649908","NEWT:410289","NEWT:373153","NEWT:3983","NEWT:352472","NEWT:1071661","NEWT:1202532","NEWT:360094","NEWT:470","NEWT:41364","NEWT:1313","NEWT:1218097","NEWT:39491","NCBITaxon:5811","NEWT:29491","NEWT:2014887","NEWT:33952","NEWT:153009","NEWT:261756","NEWT:571256","NEWT:40483","NEWT:63366","NEWT:63367","NEWT:688333","NEWT:215402","NCBITaxon:548681","NEWT:272634","NEWT:9031","NEWT:1872122","NEWT:7091","NEWT:1034015","NEWT:141262","NEWT:108931","NEWT:1055524","NEWT:4087","NEWT:9778","NEWT:306","NEWT:150475","NEWT:303","NEWT:267872","NEWT:7111","NEWT:347515","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:4090","NEWT:4092","NEWT:9541","NEWT:8694","NEWT:4093","NEWT:4096","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:941442","NEWT:536088","NEWT:13076","NEWT:1226408","NEWT:7108","NEWT:40479","NEWT:43989","NEWT:4076","NEWT:142615","NEWT:317","NEWT:1006581","NEWT:885318","NEWT:39488","NEWT:550","NEWT:4081","NEWT:273068","NEWT:554","NEWT:98334","NEWT:451516","NEWT:4084","NEWT:63577","NEWT:36185","NEWT:1225786","NEWT:7574","NEWT:1715256","NEWT:30640","NEWT:575412","NEWT:929793","NEWT:29204","NEWT:28112","NEWT:114155","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:6239","NEWT:162425","NEWT:216257","NEWT:102169","NEWT:9986","NEWT:4054","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8655","NEWT:98351","NEWT:1263854","NEWT:118503","NEWT:2059687","NEWT:160488","NEWT:28104","NEWT:207559","NEWT:407821","NCBITaxon:2","NEWT:85057","NEWT:985076","NEWT:568708","NEWT:1215323","NEWT:986","NEWT:52641","NEWT:7159","NEWT:267671","NEWT:28532","NEWT:353152","NEWT:8496","NEWT:7165","NEWT:27448","NEWT:4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