{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080233/Peptides.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080233/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080233/Capsule-deficient_Klebsiella_pneumoniae-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080233/Capsule-deficient_Klebsiella_pneumoniae-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080233/Capsule-deficient_Klebsiella_pneumoniae-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080233/CPS-intact_Klebsiella_pneumoniae-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080233/CPS-intact_Klebsiella_pneumoniae-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080233/CPS-intact_Klebsiella_pneumoniae-1.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["cyc15261284562@qq.com"],"submitter":["Yuchen Chen"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["depolymerase","virulence","capsular polysaccharides","type 3 fimbriae","biofilm","Klebsiella pneumoniae","Klebsiella pneumoniae; capsular polysaccharides; type 3 fimbriae; depolymerase; virulence; biofilm"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD080233"],"sample_protocol":["For cell and protein solution samples, SDT lysis buffer (4% SDS, 100 mM Tris-HCl, pH 7.6) was added directly. For animal tissues, samples were homogenized using an MP FastPrep-24 homogenizer (24 × 2 cycles, 6.0 M/s, 60 s) prior to the addition of SDT buffer. For plant tissues, samples were frozen in liquid nitrogen, ground with a pestle and mortar, precipitated with TCA/Acetone buffer, and then lysed in SDT buffer. All lysates (except protein solutions) were sonicated, boiled for 15 min, and centrifuged at 14,000g for 40 min. The supernatants were quantified using a BCA Protein Assay Kit. For serum or plasma samples, centrifugation at 14,000g for 20 min preceded protein quantification. An equal aliquot of 15 μg of protein from each sample was mixed with 5X loading buffer, boiled for 5 min, and separated via SDS-PAGE (4%–20% gradient gel, constant voltage 180 V, 45 min), followed by Coomassie Blue R-250 staining for quality control. For filter-aided sample preparation (FASP), each sample was reduced with 40 mM DTT at 600 rpm for 1.5 h at 37 °C, cooled to room temperature, and alkylated with 20 mM iodoacetamide in the dark for 30 min. The mixtures were transferred to 10 kDa Microcon filters, washed three times with UA buffer (8 M urea, 150 mM Tris-HCl, pH 8.0) and twice with 25 mM NH₄HCO₃. Trypsin was added at a 1:50 (trypsin:protein, w/w) ratio and incubated at 37 °C for 15–18 h. The resulting peptide filtrates were desalted on C18 cartridges, concentrated by vacuum centrifugation, and reconstituted in 40 µL of 0.1% formic acid. Peptide content was estimated via UV absorbance at 280 nm, and indexed retention time (iRT) calibration peptides were spiked into each sample for DIA experiments."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peptides were analyzed on an Orbitrap™ Astral™ mass spectrometer (Thermo Scientific) coupled to a Vanquish Neo liquid chromatography system in data-independent acquisition (DIA) mode, with MS1 scanning at 380–980 m/z (resolution 240,000 at 200 m/z) and 299 DIA windows (isolation window 2 m/z) for MS2. The raw DIA data were processed using DIA-NN (version 1.8.1) for protein identification and quantification—MaxQuant was not used in this study. The search parameters specified trypsin as the enzyme, allowing a maximum of one missed cleavage, with carbamidomethyl (C) set as a fixed modification, and oxidation (M) and acetyl (Protein N-term) as dynamic modifications. Protein identifications were filtered at a false discovery rate (FDR) of ≤ 1%. For subsequent bioinformatics, hierarchical clustering was performed using Cluster 3.0 and Java Treeview; subcellular localization was predicted via CELLO; protein domains were annotated with InterProScan/Pfam; and Gene Ontology (GO) terms and KEGG pathways were assigned using Blast2GO and local BLAST searches against appropriate databases (e.g., for Homo sapiens, Mus musculus, Rattus norvegicus, Arabidopsis thaliana, Triticum aestivum L., Oryza sativa L., Zea mays L., and Solanum lycopersicum L.). Enrichment analyses (GO and KEGG) were performed using Fisher’s exact test with Benjamini-Hochberg correction (p < 0.05). Gene Set Enrichment Analysis (GSEA) was executed using the cluster profile R package. Protein-protein interaction networks were retrieved from the STRING database and visualized in Cytoscape, with node degree calculated to evaluate protein importance. Principal component analysis (PCA) was performed using SIMCA-P following Pareto scaling. Weighted gene co-expression network analysis (WGCNA) was implemented via the WGCNA R package to identify co-expression modules. Finally, transcription factors and kinases were annotated using the Plant/Animal Transcription Factor Databases and resources including PhosphoSitePlus, Phospho.ELM, and the STRING database, depending on the species origin of the samples."],"omics_type":["Proteomics"],"labhead":["Yuchen Chen"],"instrument_platform":[""],"labhead_affiliation":["NO.2 Yabao Road, Beijing Province"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)","Klebsiella Pneumoniae"],"publication":["Not available"],"submitter_mail":["cyc15261284562@qq.com"],"submitter_affiliation":["Capital Institute of Pediatrics"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Phage depolymerase modulates virulence and biofilm in hypervirulent Klebsiella pneumoniae by CPS-mediated suppression of type 3 fimbriae","description":"Phage-derived depolymerases represent a promising antibiotic alternative for treating Klebsiella pneumoniae infections. Depolymerases can increase the sensitivity of bacteria to the host immune system and complement-mediated killing by specifically degrading capsular polysaccharides (CPS). However, the impact of depolymerases on bacterial biofilm formation remains unclear. This study found that depolymerase treatment significantly enhances the biofilm formation capability of hypervirulent K. pneumoniae (hvKp) strains, which inherently exhibit relatively weak biofilm formation due to their thick capsular polysaccharide (CPS) layers. Further investigation revealed that depolymerase-mediated CPS degradation relieved its repression on the type 3 fimbriae gene cluster mrkABCDF, thereby promoting biofilm formation. In vivo experiments in mice also showed that CPS can inhibit virulence functions associated with type 3 fimbriae. Furthermore, we found that CPS-mediated biofilm inhibition appears to be a common phenomenon among hvKp strains. In summary, by elucidating the dual role of depolymerase in modulating both virulence and biofilm in hvKp, our work reveals a potential interaction between CPS and type 3 fimbriae, providing deeper insights into the pathogenicity of this clinically important bacterium.","dates":{"publication":"2026-06-28","submission":"2026-06-26"},"accession":"PXD080233","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:1584","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","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:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:906914","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:595495","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:13037","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:2064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