{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD060098/checksum.txt"],"Xls":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD060098/plots.xls"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD060098/1165_24SP010_E_70min_2-25_trap_1ul_30ng_1_1-29-2024_19-47-42.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD060098/1167_24SP010_D_70min_2-25_trap_1ul_30ng_1_1-29-2024_21-52-02.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["Ted.Hupp@ed.ac.uk"],"submitter":["Lenka Hernychova"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Esophageal Cancer"],"software":["Not available"],"submitter_keywords":["Human","Lc-ms/ms","Oesophageal adenocarcinoma"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD060098"],"tissue":["Breast"],"sample_protocol":["GPA33:RSE-05 cross-linked proteins were purified and concentrated via SDS-PAGE. Electrophoresis was performed at 80 V for 8 minutes, followed by staining with Coomassie Brilliant Blue G-250. Gel bands were excised, washed with deionized water, and diced into small fragments. Decolorization was carried out using a freshly prepared 200 mM ammonium bicarbonate solution (NH4HCO3, pH 7.8) in 40% aqueous acetonitrile (ACN, v/v) at 30 °C for 20 minutes. The samples were then equilibrated in 50 mM NH4HCO3 (pH 7.8) containing 5% aqueous ACN (v/v) at 30°C for 30 minutes. The supernatant was removed, and the gels were dehydrated with ACN. The supernatant was removed, and the samples were reduced by the addition of 10 mM DTT at 60 °C for 60 minutes, followed by alkylation with 55 mM iodoacetamide in the dark for 45 minutes at room temperature. The supernatant was removed, and the gel pieces were washed three times with an equilibration buffer and dehydrated with acetonitrile. Trypsin digestion was carried out at 37 °C overnight using Promega sequencing-grade trypsin. Digested peptides were extracted using ACN, vacuum dried and desalted using C18 micro spin columns (Harvard Apparatus) according to the manufacturer’s guidelines. Before mass spectrometry analysis, the evaporated peptide samples were dissolved in 2% ACN (v/v) with 0.05% aqueous trifluoroacetic acid (v/v)."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["LC-MS/MS analysis was carried out using a timsTOF mass spectrometer (Bruker Daltonics) with a captive spray nanoESI (electro-spray ionization) source (Bruker Daltonics) coupled to a NanoElute 2 liquid chromatograph. The peptides were loaded into an Acclaim PepMapTM 100 nano trap column (nanoViperTM C18, 0.3 × 5 mm, 5 µm particle size, 100 Å pore size; Thermo Fisher Scientific) with mobile phase A (0.1% aqueous formic acid (v/v)) for about 2 min for desalting. Next, the peptides were eluted, at flow rate of 300 nl/min, onto an Aurora Ultimate C18 CSI (75 µm × 25 cm, 1.7 µm particle size, 120 Å pore size, IonOptics), an analytical column with integrated nanospray emitter, kept at 50 °C and separated by linear gradient elution over 64-min from 2 to 25% B and 6-min gradient from 25-48% B, followed by a 5-min wash step with 95% B. Mobile phase B was acetonitrile 100% with 0.1% formic acid (v/v). The TOF mass analyzer was operated in positive ion mode, high sensitivity mode with spray voltage of 1400 V and capillary was heated to 200°C. Acquisition method was set to PASEF (parallel accumulation, serial fragmentation) with ramp time 100 ms with close to 100% duty cycle for a total of 1.18 seconds per PASEF cycle. The master scan was acquired with mass range 100-1700 m/z and mobility range 0.7-1.4 1/K0. Precursors for MS/MS were picked at an intensity threshold of 1000. Dynamic exclusion time was set to 0.4 min. Precursor ions were then isolated with a 2-Th window for m/z < 700 and 3-Th for m/z > 700. The precursor ions were fragmented using collision-induced dissociation (CID) with collision energy as a linear ramp from 20 eV at 1/K0 = 0.6 Vs cm−2 to 59 eV at 1/K0 = 1.6 Vs cm−2  Spectra were analyzed for DSS cross linked adducts as previously reported in the Singh et al paper (36)."],"omics_type":["Proteomics"],"labhead":["prof. Ted Hupp"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Institute of Genetics and Cancer (IGC), University of Edinburgh, Edinburgh, Scotland"],"species":["Homo Sapiens (human)"],"publication":["41808009 Brydon J, Krejcir R, Zavadil-Kokas F, Singh A, Henek T, Hernychova L, Coleman S, Al Shboul S, Hrabal V, Kuncova Z, Mayordomo MY, Arcimowicz Ł, Ball KL, Padariya M, Kalathiya U, Vojtesek B, Hupp T, O'Neill JR. GPA33 forms a distinct diagnostic target class to Claudin 18.2 in oesophageal adenocarcinoma enabling the development of a novel GPA33 antibody-based detection platform. Cell Mol Biol Lett. 2026 31(1):58 10.1186/s11658-025-00852-1"],"submitter_mail":["lenka.hernychova@mou.cz"],"submitter_affiliation":["Masaryk Memorial Cancer Institutre, Zluty kopec 7, Brno 656 53, Czech Republic"],"submitter_country":["Czechia"],"pubmed_abstract":["<h4>Background</h4>Oesophageal adenocarcinoma (OAC) is a cancer of high unmet clinical need. Because of tumour heterogeneity, it is likely that OAC will be stratified into several subtypes. Claudin 18.2 antibodies form emerging novel therapeutics in patients with a subtype of OAC. A large-scale proteogenomics screen in OAC identified glycoprotein A33 (GPA33) protein as a dominating cancer-specific target. We set out to determine whether GPA33 is distinct from or overlaps with Claudin 18.2 as a theranostic target in OAC.<h4>Methods</h4>A microarray from n = 106 patients, composed of cancer, normal squamous tissue, normal gastric tissue, and metastatic lymph nodes, was used to compare the expression of GPA33 and Claudin 18.2. A single-chain variable fragment (scFv)-phage display library was screened against recombinant GPA33 protein to isolate novel monoclonal antibodies. Next-generation complementarity-determining region 3 (CDR3) DNA sequencing (NGS) and enzyme-linked immunosorbent assay (ELISA) were both used to measure efficacy of antibody enrichment during biopanning.<h4>Results</h4>GPA33 exhibits superior tumour-specific expression compared with Claudin 18.2, the latter of which is expressed in normal gastric tissue. GPA33 and Claudin 18.2 exhibit statistically significant mutually exclusive expression in cancer tissue cores; 36% of cancers are GPA33<sup>+</sup>/Claudin 18.2<sup>-</sup>, whilst 22% are GPA33<sup>-</sup>/Claudin 18.2<sup>+</sup>. GPA33 therefore forms a novel target for theranostics in a significant number of patients. A monoclonal antibody (RSE-05) targeting GPA33 was isolated from a scFV-phage display library. The antibody required a di-sulphide bridge to maintain its epitope on the antigen. Epitope mapping was performed using di-sulphide bridge mutagenesis, peptide-phage display, and XL-MS. The dominant epitope resides in the V-type IgG domain of GPA33 at residues 27-29 and structural amino acids S17 and K65. This di-sulphide bridge-constrained epitope defines a novel monoclonal antibody binding interface. The RSE-05 monoclonal antibody can be adapted and used as a capture-sensor tool to measure GPA33 protein in liquid phase using a two-site sandwich ELISA format.<h4>Conclusions</h4>GPA33 exhibits elevated cancer-specific expression relative to Claudin 18.2, indicating that GPA33 can also form the basis for a cancer diagnostic. Claudin 18.2 and GPA33 generally exhibit mutually exclusive expression suggestive of two different OAC development pathways. Thus, GPA33 forms a novel target that captures the Claudin 18.2-negative patient class, and the monoclonal antibody we describe forms the basis for novel diagnostic and therapeutic tools for development in OAC."],"pubmed_title":["GPA33 forms a distinct diagnostic target class to Claudin 18.2 in oesophageal adenocarcinoma enabling the development of a novel GPA33 antibody-based detection platform."],"pubmed_authors":["Brydon Jack J, Krejcir Radovan R, Zavadil-Kokas Filip F, Singh Ashita A, Henek Tomas T, Hernychova Lenka L, Coleman Skye S, Al Shboul Sofian S, Hrabal Vaclav V, Kuncova Zuzana Z, Mayordomo Marcos Yébenes MY, Arcimowicz Łukasz Ł, Ball Kathryn L KL, Padariya Monikaben M, Kalathiya Umesh U, Vojtesek Borivoj B, Hupp Ted T, O'Neill J R JR"],"additional_accession":[]},"is_claimable":false,"name":"Isolation of a novel GPA33 monoclonal antibody that detects a redox regulated epitope","description":"Membrane receptor targets have been identified using proteogenomics platforms in oesophageal adenocarcinoma (OAC) that are specific for tumour compared to normal adjacent oesophageal and gastric tissue. One of these receptors, GPA33, is expressed in patients including involved lymph nodes suggesting it might form a clinically relevant diagnostic and/or therapeutic target. We have used a massively diverse scFv-phage display library to identify recombinant scFv sequences enriched during biopanning against native GPA33 using both next-generation CDR3 DNA sequencing and functional ELISA. One active scFV, redox-sensitive epitope 05 (RSE-05), was converted using gene synthesis into a single cistronic full-length IgG expression plasmid containing a self-cleavage site in between the heavy and light chain. The recombinant RSE-05 MAB can bind to the outer surface of living, non-permeabilized adherent MCF7 cells transfected with the full-length GPA33 gene as defined by immunofluorescence or flow cytometry. Unexpectedly, the inclusion of DTT in a pre-incubation stage abrogated RSE-05 MAB binding using immunoblotting, suggesting that disulphide bridges form the native epitope.   GPA33 is composed of two IgG-like lobes, containing three disulphide bonds. Mutation of the disulphide bridge at C22S or C96S in Lobe 1 abolishes RSE-05 MAB binding in a native immuno dotablot suggesting this lobe forms the primary epitope. Peptide-phage display of the RSE-05 MAB identified a linear epitope within Lobe 1.  Cross-linking mass spectrometry (XL-MS) using DSS identified a motif in FR2/CDR2 of the IgG that forms a covalent bond with S27, which is consistent with the core epitope motif (27-STS-29) identified by peptide-phage display.  XL-MS also identifed a covalent bond between Lobe 1 and Lobe 2 and suggesting that the GPA33 protein can exist in two confromational states. Accordingly, mutation of Cysteine residues in Lobe 2 abolishes the binding of RSE-05 MAB in a denaturing immunoblot, suggesting that disruption of the conformational integrity of Lobe 2 can imapct on the presumed primary epitope formed by the C22-C96 disulphide.  Immunohistochemistry of an oesophageal cancer tumour microarray indicated that higher tumor grades, lymph node involvement, and venous invasion are associated with higher CD3, CD8, and GPA33 scores, indicating a potential link between immune response and tumor aggressiveness. Together, these data identify a novel monoclonal antibody that contacts a redox regulatable epitope in GPA33 protein and that can be used to study allosteric interactions in the GPA33 protein.  This biologic might also form a novel diagnostic and therapeutic biologic for use in metastatic upper GI cancers.","dates":{"publication":"2026-04-27","submission":"2025-01-23"},"accession":"PXD060098","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:2003758","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:9900","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:9979","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1774208","NEWT:8644","NEWT:1125630","NEWT:202914","NEWT:222523","NEWT:27602","NEWT:502779","NEWT:297246","NEWT:483139","NEWT:101491","NEWT:8639","NEWT:863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