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Maes"],"software":["Not available"],"tissue":["Vesicle","Cell Culture"],"sample_protocol":["Thawed sEV lysates were sonicated three times for five seconds using a VC–50 Vibra cell ultrasonic processor (Sonics & Materials Inc., Newtown, CT, USA) at an output of 30 W. Lysates were centrifuged at 12,000 x g for ten minutes at 4 °C, with supernatants collected. Aliquots (100 µL) were precipitated using methanol/chloroform as described in Wessel and Flügge [44]. Air-dried protein pellets were resuspended in 100 μL of ammonium bicarbonate (10 mM). Protein concentrations were determined using Qubit 1.0 fluorometer (Invitrogen, ThermoFisher Scientific) and a QuDye protein quantification kit (Lumiprobe).An aliquot of 50 µg of proteins (3 µg/μL) were reduced by addition of 1 μL of 200 mM dithiothreitol, and incubation in darkness at 56 °C for forty–five minutes in a thermomixer (Eppendorf AG). Proteins were alkylated by addition of 1 μL of 200 mM iodoacetamide in 0.1 M ammonium bicarbonate, and incubation in darkness at room temperature (~20°C) for thirty minutes in a thermomixer. Proteins were digested by addition of 1 μL of MS–grade Pierce™ trypsin/Lys–C protease mix (ThermoFisher Scientific) (1:50 enzyme:protein), 5 μL of acetonitrile, and incubation overnight at 37 °C in a thermomixer. The resulting peptides were desalted with Pierce™ 100 μL C18 Tips (ThermoFisher Scientific), dried using a centrifuge concentrator and resuspended in 0.1% formic acid prior to LC–TIMS-MS/MS analysis."],"repository":["Pride"],"labhead":["Evelyne Maes"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Bioeconomy Science Institute, AgResearch Ltd., Lincoln 7674, New Zealand."],"publication":["42182006 Pratt JT, Lake AVR, Maes E, Thomas A, Hefer C, Mitchell MD, Heiser A, Ross MA. &lt;i&gt;Mycoplasma bovis&lt;/i&gt; infection alters small extracellular vesicle cargo derived from bovine endometrial epithelial cells cultured in static bioreactors. Front Microbiol. 2026 17:1770401 10.3389/fmicb.2026.1770401"],"submitter_affiliation":["Agresearch"],"labhead_mail":["evelyne.maes@agresearch.co.nz"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Primary Bacterial Infectious Disease"],"submitter_keywords":["Bioreactor","Small extracellular vesicles","Proteomics","Mycoplasma bovis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD076118"],"quantification_method":[""],"modification":[""],"data_protocol":["The PEAKS Online software package (Bio informatic Solutions Inc) was used to analyse the LC-TIMS-MS/MS data. Raw data were refined by a built-in algorithm that enabled association of chimeric spectra. Proteins/peptides were identified with the following parameters: precursor mass error tolerance of 20 ppm, fragment mass error tolerance of 0.05 Da, in-house database with Bos taurus and M. bovis (UNC_01) (v2020.06, 65878 sequences), Saccharomyces cerevisiae Uniprot database (v2022.01, 6638 sequences) as a contaminant database, trypsin/LysC specified as digestive enzyme and up to two missed cleavages were allowed. Carbamidomethylation of cysteine was set as fixed modification. Oxidation (M), carbamylation (C) and deamidation (NQ) are chosen as variable modifications. A maximum of three post-translational modifications per peptide were permitted. False discovery rate (FDR) estimation was made based on decoy-fusion. An FDR of 1 % was set at peptide level and a -10–log p> 20 at protein level, with at least one unique peptide per protein considered adequate for confident protein identification. 1.6.4 Label free quantification Label-free quantification was performed using the quantitation node of Peaks Online software, enabling comparison of protein expression levels between the distinct groups. Alignment used a mass-tolerance error of 20 ppm, and a maximum retention-time shift tolerance of two minutes. Relative protein and peptide abundances in RT-aligned samples were determined by peptide-feature-based quantification. All samples were normalised using total ion chromatogram normalisation relative to a quality control sample, and identity transfer within groups was allowed. Relative comparison between samples is based on the area under the curve. Relative comparisons between samples were based on the cumulative area under the curve, calculated from unique peptides assigned to each protein, which were limited to the top 10 highest-quality peptides. The FDR was set at 1 %.Principle component analysis (PCA) was performed on protein abundance levels using the PCA function of the mixOmics package [45]. Prior to calculating PCA, proteins were filtered to only include those with an abundance estimate of at least 25 % within each group. Protein differential abundance analyses were calculated by fitting a negative binomial model (glm.nb from the R package MASS (Core Team, 2013; Venables & Ripley, 2013) to estimate the abundance as an interaction between the protein and sample group, followed by the adjusted p–value calculation for each individual protein in each group using the R package predictmeans (version 1.0.6, ([46]).Principle component analysis (PCA) was performed on protein abundance levels using the PCA function of the mixOmics package [45]. Prior to calculating PCA, proteins were filtered to only include those with an abundance estimate of at least 25 % within each group. Protein differential abundance analyses were calculated by fitting a negative binomial model (glm.nb from the R package MASS (Core Team, 2013; Venables & Ripley, 2013) to estimate the abundance as an interaction between the protein and sample group, followed by the adjusted p–value calculation for each individual protein in each group using the R package predictmeans (version 1.0.6, ([46])."],"omics_type":["Proteomics"],"species":["Bos Taurus (bovine)","Metamycoplasma"],"submitter_mail":["evelyne.maes@agresearch.co.nz"],"submitter_country":["New Zealand"],"doi":["10.6019/PXD076118"],"pubmed_abstract":["<i>Mycoplasma bovis</i> (<i>M. bovis</i>) is a pathogenic bacterium that causes significant production losses and welfare challenges in cattle. Eradication is challenging as <i>M. bovis</i> can infect host cells intracellularly, reducing detection from immunomodulatory cells. With an aim to improve diagnostics for post-eradication surveillance, small extracellular vesicles (sEVs) were used to identify novel biomarkers of <i>M. bovis</i> infection. Readily accessible in body fluids, these nanoparticles encapsulate protein cargo indicative of the metabolic state of their tissue of origin. Here, we developed a novel three-dimensional <i>in vitro</i> cell culture model using static bioreactors to investigate changes in host cell (bovine endometrial epithelial cells) sEV protein cargo during <i>M. bovis</i> infection. Three-dimensional cell culture modelling better mimics native tissue architecture than two-dimensional modelling, enhancing intercellular function and physiological relevance. Size exclusion chromatography columns were used to isolate sEVs from control and co-culture bioreactor flasks. Liquid chromatography-trapped ion mobility spectrometry-tandem mass spectrometry was used to investigate the proteome of sEVs. Differential proteome profile analysis resulted in 193 proteins that demonstrated significantly different abundance (<i>p</i> < 0.05) in sEVs (co-culture vs. control cells), with changes to host Histone proteins the most prominent. Most <i>M. bovis</i>-derived proteins were those involved in cellular metabolism with enrichment of proteins classified under glycolysis. However, owing to their reduced genome, several glycolytic enzymes in <i>Mycoplasma</i> spp. are multifunctional and contribute to pathogenesis through involvement in adhesion and invasion of host cells. Homologs of immunoreactive <i>M. bovis-</i>lipoproteins were present in the proteome of co-culture sEVs. Host-derived proteins were consistent with those linked with infection and sEV trafficking. Our study indicated that sEV protein cargo was altered by <i>M. bovis</i> infection, with results providing an important insight into sEV biology in the context of bacterial infection."],"pubmed_title":["&lt;i&gt;Mycoplasma bovis&lt;/i&gt; infection alters small extracellular vesicle cargo derived from bovine endometrial epithelial cells cultured in static bioreactors."],"pubmed_authors":["Pratt Joel T JT, Lake Alice V R AVR, Maes Evelyne E, Thomas Ancy A, Hefer Charles C, Mitchell Murray D MD, Heiser Axel A, Ross Mallory A MA"],"additional_accession":[]},"is_claimable":false,"name":"Development of an in vitro model of Mycoplasma bovis infection in static bioreactors for proteomic investigation of small extracellular vesicles for biomarker discovery","description":"Mycoplasma bovis (M. bovis) is a pathogenic bacterium that causes significant production and welfare issues in cattle. The dairy industry is essential to New Zealand, contributing over a quarter of the country’s total exports. Each year, ~4.7 million cows produce ~20.5 billion litres of milk, which is worth ~$23 billion NZD to the New Zealand economy. An unregulated M. bovis outbreak would be catastrophic for the country. Eradication is challenging as M. bovis can infect host cells intracellularly, reducing detection from immunomodulatory cells. With an aim to improve diagnostics for post-eradication surveillance, small extracellular vesicles (sEVs) were used to identify novel biomarkers of M. bovis infection. Readily accessible in body fluids, these nanoparticles encapsulate protein cargo indicative of the metabolic state of their tissue of origin. Here, we developed a three-dimensional in vitro cell culture model using static bioreactors to investigate changes in host cell sEV protein cargo during M. bovis infection. Size exclusion chromatography columns were used to isolate sEVs from control and co-culture bioreactor flasks. Liquid chromatography-trapped ion mobility spectrometry-tandem mass spectrometry (LC–TIMS-MS/MS) was used to investigate the proteome of sEVs.","dates":{"publication":"2026-06-01","submission":"2026-03-25"},"accession":"PXD076118","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","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:488003","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:156587","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:65121","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","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:272831","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:291146","NEWT:233271","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:3735","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:9030","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:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","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","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","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:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4233","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: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