{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-2vs1.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/checksum.txt"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-2vs1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-2vs1.msfView"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-2-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-2-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-1-4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-1-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-2-4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-2-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-1-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-1-1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/LBW-0428.pdStudy","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-2vs1.pdResultView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/0429-LBW-2vs1.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062992/LBW-0428.pdStudy.bak"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["huochy5@mail.sysu.edu.cn"],"submitter":["Chuying Huo"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Malignant Neoplasm Of Ovary"],"software":["Not available"],"submitter_keywords":["Vista","Neutrophils","Chemoresistance","Cd8+ t cell","High-grade serous ovarian cancer"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062992"],"tissue":["Ovarian Serous Carcinoma Cell"],"sample_protocol":["Protein extraction from tumor tissues After NACT-IDS or PDS with postoperative adjuvant chemotherapy, treatment efficacy was assessed according to NCCN guidelines5. For primary tumor, patients who relapsed 6 months or more after initial chemotherapy were termed platinum-sensitive5. In contrast, patients whose disease recurred in less than 6 months were classified as platinum-resistant5. The fresh tumor samples from 4 pairs of platinum-resistant and platinum-sensitive HGSOC patients were processed by manually dissecting, freeze grinding, and ultrasonication. In parallel, tissue protein extraction was facilitated by employing RIPA buffer enriched with a cocktail of protease and phosphatase inhibitors to ensure comprehensive lysis. The lysates were then subjected to high-speed centrifugation at 4°C to sediment insoluble materials, allowing for the collection of the supernatant, which constitutes the protein-rich cell lysate. The protein concentration within the lysates was quantified using a BCA protein assay kit (CWBIO, Jiangsu, China).  Proteolysis, desalinization and Nano-LC-MS/MS The extracted proteins were first treated with a reducing agent, 2 mM dithiothreitol, and incubated at 56°C for 30 minutes and then alkylated using 10 mM iodoacetamide at ambient temperature for 30 minutes. Following this, the proteins were digested into peptides with trypsin at a ratio of 1:50 for 16 hours at 37°C. The resulting peptides were then purified by passing them through SepPak C18 cartridges (Waters, MA) and dried under vacuum using a Speed Vac concentrator. For mass spectrometric analysis, the peptides were resuspended in solvent A (0.1% formic acid) and introduced into an EASY-nLC 1200 liquid chromatography system, which was interfaced with an Orbitrap Fusion mass spectrometer (Thermo Fisher Scientific). The peptides were separated on a 75 μm ×150 mm capillary column packed with 1.9 μm C18 AQ stationary phase using a gradient of 8-38% acetonitrile (ACN) in 0.1% formic acid over a period of 120 minutes at a flow rate of 300 nL/min. Mass spectrometry data was acquired with an MS1 scan ranging from 350 to 1800 m/z at a resolution of 60,000, using 100% automatic gain control (AGC). This was complemented by MS/MS acquisition in a data-dependent manner using higher-energy collisional dissociation (HCD) in the ion trap with an injection time of 35 ms and 100% AGC. Mass spectrometry analysis was performed by the Bioinformatics and Omics Center, Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Mass spectrum data processing and analysis Data processing was primarily conducted by using R studio software (version 4.4.0). Firstly, we used the ‘VIM’ package to assess the dataset for missing values. Subsequently, according to classification and regression trees, we utilized the ‘mice’ package to perform multiple imputations for the missing data and standardized the dataset to ensure consistency and comparability across variables. To identify differentially expressed proteins (P < 0.05, |logFC| > 1.5) between groups, both the ‘edgeR’ and ‘limma’ packages were employed. For the enrichment analysis and visualization of Gene Ontology (GO) and Gene Set Enrichment Analysis (GSEA), we engaged packages such as ‘ggplot2’, ‘clusterProfiler’, ‘org.Hs.eg.db’, ‘ReactomePA’, ‘tidyverse’, ‘biomaRt’, ‘enrichplot’, as well as the Cytoscape software. To pinpoint the differentially expressed proteins (DEPs) correlated with Neus, we referenced a neutrophil gene set from the literature and intersected it with the DEPs derived from edgeR and limma differential analyses. Ultimately, we identified three significant neutrophil-related DEPs that were potentially associated with platinum-resistance in HGSOC patients."],"omics_type":["Proteomics"],"labhead":["Chuying Huo"],"instrument_platform":[""],"labhead_affiliation":["The Sun Yat-sen Memorial Hospital of the Sun Yat-sen University"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["10.1158/2326-6066.CIR-25-1118"],"submitter_mail":["huochy5@mail.sysu.edu.cn"],"submitter_affiliation":["Sun Yat-sen Memorial Hospital"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"VISTA+ Neutrophils Enhance Chemoresistance in High-Grade Serous Ovarian Cancer by Suppressing CD8+ T Cells Infiltration","description":"Platinum-based chemoresistance is a primary cause of treatment failure and unfavorable prognosis in high-grade serous ovarian cancer (HGSOC). Although inflammation plays a critical role in chemoresistance, in which neutrophils (Neus) emerge as potent inflammatory regulator across various cancers, the precise mechanisms linking Neus to chemoresistance in HGSOC patients are not well understood. Here, we conducted a retrospective review of HGSOC patients treated with adjuvant chemotherapy, analyzing clinicopathological data and laboratory parameters to show a significant correlation between neutrophil-to-lymphocyte ratio and chemotherapy efficacy. Further experiments revealed an increase in Neus among chemoresistant patients. Proteomic analysis and single-cell RNA sequencing identified VISTA+ Neus as a potent prognostic predictor. In vivo, VISTA blockade reduced VISTA+ Neus infiltration, but increased CD8+T cells within tumor tissues, thereby enhancing chemosensitivity. Our findings highlight the role of VISTA+ Neus in chemoresistance and suggest that targeting these cells could be a novel therapeutic strategy to enhance chemosensitivity in 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