{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/EVtrap.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/SEC.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/ultracentrifugation.xlsx"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/20240613-DDA-YWJ-293F-9-Sample-TEST-1.db.proteins.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/20220929-DDA-STX7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/EVtrap.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/20220929-DDA-PTGFRN.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/ultracentrifugation.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/SEC.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/20220929-DDA-Lamp2b.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/20220929-DDA-CXADR.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/20220929-DDA-SNAP23.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/20220929-DDA-Rab7a.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/20220929-DDA-EPCAM.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/20220929-DDA-ENPP1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057965/20220929-DDA-PDL1.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["shizhiwang2009@seu.edu.cn"],"submitter":["Wenjing Yan"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":["Lc-s/ms","Expi293f-evs"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057965"],"tissue":["Cell Culture"],"sample_protocol":["We employed three different and independent strategies to isolate Expi293F-EVs: ultracentrifugation, magnetic bead-based EVtrap technology, and a purification process integrating tangential flow industrial extraction 35 with size exclusion chromatography."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The raw data were searched using Proteome Discoverer 2.3 software, configured with trypsin/P as the enzyme, allowing up to 3 missed cleavages. Fixed modifications included carbamoyl methylation (+57.02 Da), while variable modifications encompassed methionine oxidation (+15.99 Da) and acetylation (+42.01 Da). Both protein and peptide false discovery rates (FDRs) were set to 1% to ensure high data quality."],"omics_type":["Proteomics"],"labhead":["Wang shi zhi"],"instrument_platform":[""],"labhead_affiliation":["Key Laboratory of Environmental Medicine Engineering, Ministry of Education, School of Public Health, Southeast University, Nanjing, China."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["13915963122@163.com"],"publication":["41807391 Yan W, Wang S, Hao H, Lin H, Wang C, Xie S, Zhang X, Lu Y, Ding X, Chen X, Liu H, Zhang G, Wei D, Ma C, Tang C, Li X, Yu B, Hu J, Gu Z, Yu EY, Li W, Xia J, Zhang H. Extracellular vesicle engineering using a small scaffold protein. Nat Commun. 2026 17(1):3726 10.1038/s41467-026-70451-x"],"submitter_affiliation":["Southeast university"],"submitter_country":["China"],"pubmed_abstract":["Extracellular vesicles (EVs) are promising drug-delivery vehicles owing to their biocompatibility and low immunogenicity. Genetic engineering of a membrane-bound EV-sorting scaffold protein empowers EVs by installing targeting moieties on the surface and enriching therapeutic cargo in the lumen. However, the choice of scaffold proteins with simple structures and short sequences is limited. Here, we conduct mass spectrometry-based proteomic studies and identify ENPP1 as a superior scaffold protein. Furthermore, we show that a truncated 144-amino acid variant, EN144, efficiently loads diverse therapeutic cargoes and outperforms conventional scaffolds. By fusing EN144 to the IL-6 decoy receptor gp130, we create engineered decoy EVs that potently inhibit inflammatory IL-6 trans-signaling. In mouse models, these EVs reduce inflammation, improve survival in sepsis, and, when targeted to cartilage, alleviate tissue damage in osteoarthritis. Our work establishes EN144 as a minimal, high-performance scaffold for EV engineering and demonstrates its broad therapeutic potential for inflammatory diseases."],"pubmed_title":["Extracellular vesicle engineering using a small scaffold protein."],"pubmed_authors":["Yan Wenjing W, Wang Shizhi S, Hao Haibin H, Lin Hong H, Wang Chen C, Xie Shuqian S, Zhang Xing X, Lu Yiran Y, Ding Xin X, Chen Xue X, Liu Haohan H, Zhang Guiyuan G, Wei Dong D, Ma ChangYan C, Tang Cheng C, Li Xiuting X, Yu Bingjia B, Hu Jing J, Gu Zhongze Z, Yu Evan Yi-Wen EY, Li Weiqin W, Xia Jiang J, Zhang Hao H"],"additional_accession":[]},"is_claimable":false,"name":"Identification of a 144-amino-acid Scaffold Protein for Extracellular Vesicle Engineering","description":"Extracellular vesicles (EVs) have emerged as promising drug-delivery vehicles. Genetic engineering of a membrane-bound, EV-sorting scaffold protein empowers these cell-borne nanosized vesicles by installing targeting moieties on the surface and enriching therapeutic cargo in the lumen. However, the choice of scaffold proteins with a simple structure and short sequence is scarce. Here, we conduct mass-spectrometry-based proteomic studies, identify 15 candidate proteins with EV-sorting properties, and examine their capability as the scaffold protein. ENPP1 stands out from our screening, outperforming the widely used EV-sorting proteins PTGFRN and Lamp2b with high abundance, homogeneity, stability, and engineerability. In particular, a 144-amino acid truncated version of ENPP1, called EN144 here, demonstrates high-density loading of cargos, including peptides, proteins, and mRNAs. Based on this finding, we engineer decoy EVs expressing IL-6 signal transducer (IL6ST, a.k.a. gp130) fused with EN-144, EN144-EVhgp130, to inhibit the IL-6 trans-signaling pathway. The resulting decoy EVs elicit potent anti-inflammatory effects and improve the survival rate of septic mice. Chondrocyte-targeting EN144-EVhgp130 ameliorates inflammation and remodels the synovial tissue microenvironment of cartilage in a rat model of osteoarthritis (OA), surpassing tocilizumab (TCZ), the clinically approved humanized anti-interleukin-6 receptor (IL-6R) antibody. Altogether, we report the identification and verification of EN144 as one of the smallest and simplest scaffold proteins for EV engineering and showcase systematic and local administrations of EN144-engineered decoy EVs for treating inflammatory 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