{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD055136/Protein_Vordalii_final.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD055136/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD055136/V6_Bacteria3_Slot1-33_1_322.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD055136/V3_OMV3_Slot1-30_1_319.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD055136/V5_Bacteria2_Slot1-32_1_321.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD055136/V4_Bacteria1_Slot1-31_1_320.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD055136/V1_OMV1_Slot1-28_1_317.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD055136/V2_OMV2_Slot1-29_1_318.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["ravendano@unab.cl"],"submitter":["Guillermo Nourdin"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Salmonids","Proteome","Vibriosis","Omvs."],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD055136"],"sample_protocol":["1 Protein extraction for nLC-MS / MS Each replicate of the Vo-LM-18 cells and OMVs suspension were lyophilized overnight. Subsequently, each sample was resuspended in 500 µL of 8 M urea with 25 mM sodium bicarbonate and sonicated for 1 min with 3 pulses of 9 seconds at 40% intensity. Finally, the samples were centrifuged at 10,000 x g for 10 min discarding the pellet and storing the supernatant at -80 °C.  2 Protein extraction and digestion for nLC-MS / MS The proteins of each sample were subjected to precipitation using 5:1 v/v cold acetone 100% and incubated overnight at -20 °C, then they were centrifuged at 15,000 x g for 10 min; the supernatant was discarded, and the pellet was washed three times with acetone at 90% v/v, dried in a rotary concentrator at 4 °C, and finally was resuspended in 8 M urea with 25 mM of ammonium bicarbonate (NH4HCO3, pH 8.0). The proteins were quantified with Qubit protein assay, where 100 µg were reduced with 20 mM dithiothreitol for 60 min, alkylated with 20 mM iodoacetamide in the dark for 60 min, diluted ten times with 25 mM of ammonium bicarbonate pH 8.0 and digested with trypsin/LyC (Promega, Madison, WI, USA) in a 1:50 ratio overnight at 37 °C. Peptides were cleaned using Pierce C-18 Spin Columns (Thermo Scientific, USA) according to the manufacturer’s instructions, and the eluted peptides were dried using a rotary concentrator at 4 °C, and resuspended in 2% acetonitrile with 0.1% (v/v) formic acid (Merck, Germany), and quantified using Direct Detect Spectrometer (Merck Millipore).  3 Liquid chromatography A nanoElute® liquid chromatography system (Bruker Daltonics) was used, and peptides (200 ng of digest) were separated within 90 min at a flow rate of 400 nL/min on a reversed-phase column Aurora Series CSI (25 cm x 75µm i.d. C18 1.6 µm) (IonOpticks, Australia) with 50 °C. Mobile phases A and B were water and acetonitrile with 0.1% (v/v) formic acid, respectively. The B percentage was linearly increased from 2 to 17% within 57 min, followed by an increase to 25% B within 21 min and further to 35% within 13 min, followed by a washing step at 85% B and re-equilibration.  4 The timsTOF Pro mass spectrometer All samples were analyzed three biologicals replicated for condition on a hybrid Trapped Ion Mobility Spectrometry (TIMS) quadrupole time-of-flight mass spectrometer (MS) (TIMS-TOF Pro, Bruker Daltonics) via a CaptiveSpray nano-electrospray ion source. The MS was operated in data-dependent mode for the ion mobility-enhanced spectral library generation. We set the accumulation and ramp time was 100 ms each and recorded mass spectra in the range from m/z 100–1700 in positive electrospray mode. The ion mobility was scanned from 0.6 to 1.6 Vs/cm². The overall acquisition cycle of 1.16 s comprised one full TIMS-MS scan and 10 parallel accumulation-serial fragmentation (PASEF) MS/MS scans."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Database searching Tandem mass spectra were extracted by TIMS Control v2.0. Charge state deconvolution and deisotoping were not performed. All MS/MS samples were analyzed using PEAKS Studio (Bioinformatics Solutions, Waterloo, ON Canada; v10.5 [2019-11-20]). PEAKS Studio was set up to search the UniProt_SwissProt Vibrio ordalii database (3,390 entries) assuming the digestion enzyme trypsin. PEAKS Studio was searched with a fragment ion mass tolerance of 0,050 Da and a parent ion tolerance of 50 PPM. Carbamidomethyl of cysteine was specified in PEAKS Studio as a fixed modification. Deamidated of asparagine and glutamine, oxidation of methionine, acetyl of the n-terminus and carbamyl of lysine and the n-terminus were specified in PEAKS Studio as variable modifications.   LFQ and differential expression analysis Individual identification reports from PEAKS were concatenated, and missing values (NA) resultant was imputed by MICE (van Buuren & Groothuis-Oudshoorn, 2010). To determine which proteins were differentially and significantly expressed in the treatments contrast we applied a Wald test to data with a Benjamini-Hochberg correction using Deseq2 (Love et al., 2014). Any protein associated with p-adjust < 0.05 is considered significant. The identification of Differentially Expressed Proteins (DEPs) was carried out by comparing the expression ratio of proteins identified in OMVs versus bacteria (OMVs/bacteria). Graphics representations related to quantification results were created using statistical environment R (R Core Team, 2019). with EnhancedVolcano (Blighe, 2018), Complex Heatmap v.2.0.0 (Gu et al., 2016), GOplot (Walter et al., 2015) and R base packages. In addition, prediction of the subcellular localization of the proteins identified in OMVs and bacteria was carried out through PSORTb v3.0 using default parameters (Yu et al., 2010).   Sequence protein annotation was performed by Sma3s (Casimiro‐Soriguer et al., 2017) with default parameters. The Protein-Protein Interaction was done by mapping protein sequence against Vibrio anguillarum in STRING database (Szklarczyk et al., 2021). The resulting network was importing and processed in Cytoscape v.3.91 (Shannon et al., 2003)."],"omics_type":["Proteomics"],"labhead":["Ruben Avendaño-Herrera"],"instrument_platform":[""],"labhead_affiliation":["Universidad Andrés Bello, Laboratorio de Patología de Organismos Acuáticos y Biotecnología Acuícola, Facultad de Ciencias de la Vida, Viña del Mar, Chile"],"submission_type":["PARTIAL"],"species":["Vibrio Ordalii"],"publication":["10.3390/ANI14243598"],"submitter_mail":["gnourdin@melisainstitute.org"],"submitter_affiliation":["MELISA Institute"],"submitter_country":["Chile"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic analysis of the fish pathogen Vibrio ordalii strain Vo-LM-18 and its outer membrane vesicles","description":"Vibrio ordalii is the causative agent of atypical vibriosis in salmonids cultured in Chile. While extensive research has provided valuable insights into V. ordalii through phenotypic, antigenic, and genetic typing, as well as various virulence mechanisms (e.g., capsular material, iron-uptake systems, and outer membrane vesicles [OMVs]), proteomic characterization remains largely unexplored. This study aimed to advance the proteomic knowledge of Chilean V. ordalii Vo-LM-18 and its OMVs, which have been extensively characterized in several studies and have demonstrated their virulence. Using Nano-UHPLC-LC-MS/MS, we identified 2,242 proteins in the bacterium and 1,755 proteins in its OMVs. Among these, 644 unique proteins were detected in V. ordalii Vo-LM-18, 156 unique proteins were found in its OMVs, and 1,596 proteins were shared between both components.  bioinformatics compartment prediction (PSORT algorithm) revealed that the major categories in the OMVs were similar to those in the bacteria (i.e., cytoplasmic and cytoplasmic membrane proteins), though with different proportions. Functional annotation with Gene Ontology identified 37 biological pathways in V. ordalii Vo-LM-18 and 28 in its OMVs. Proteins associated with transport, transcription, and virulence were predominant in both the bacteria and the vesicles. Comparison between the strain Vo-LM-18 and its OMVs showed evident differences in protein expression, with OMVs expressing a higher number of virulence-associated proteins, including those related to iron- and heme-uptake mechanisms. Notable pathways in the bacteria included flagellum assembly, heme group-associated proteins, and protein biosynthesis. This proteomic analysis also represents the first detection of RTX toxin in a V. ordalii strain (Vo-LM-18) and its vesicles. Our results highlight the crucial role of OMVs in the pathogenesis and adaptation of V. ordalii, suggesting their potential as diagnostic biomarkers and therapeutic targets for bacterial infections.","dates":{"publication":"2026-05-14","submission":"2024-08-23"},"accession":"PXD055136","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","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:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","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:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","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:44685","NEWT:161934","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:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","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:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","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:906914","NEWT:9031","NEWT:27292","NEWT:1050722","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:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","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:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:40674","NEWT:1194669","NEWT:443906","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:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:48106","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:3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