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D M Santos"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Fungal extracellular","ultracentrifugation","profiles","Fungal extracellular; vesicles; ultracentrifugation; profiles","vesicles"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD076414"],"sample_protocol":["Preparation of EV samples for proteomics. EVs from C. deuterogattii R265, C. auris MMC2 and C. parapsilosis GA1 were fractionated by sequential centrifugation as described before in this section to generate biological triplicates. Samples were lysed with 0.1 mm zirconium beads (1:1, v/v) followed by five cycles of agitation (1 min each), interspersed with 1-min cooling intervals, using the bead beater L-BEADER (Loccus). Subsequently, 8 M urea was added to the pellet, and the lysis process was repeated for five cycles under the same conditions. The lysates were centrifuged at 18,000 × g at 4 °C for 15 min, supernatants were collected, and protein concentrations were determined by fluorometric quantification using a Qubit fluorometer (Thermo Fisher Scientific Inc.). Samples containing 100 µg of protein were reduced with dithiothreitol (DTT; final concentration 10 mM) for 30 minutes at 56°C. Samples were cooled to room temperature and alkylated with 15 mM iodoacetamide for 25 minutes in the dark. The solution was then incubated again with 10 mM DTT for 15 minutes at room temperature in the dark. Protein samples were diluted with 50 mM ammonium bicarbonate (ABC) to reduce the urea concentration to 2 M, and pH was adjusted to 7-8. Samples were then enzymatically digested with trypsin (1:50, w/w) and incubated overnight at 37°C. Following digestion, trifluoroacetic acid (TFA) was added to a final concentration of 0.5% and the digested proteins were quantified again with the Qubit system (Thermo Fisher Scientific Inc.). Peptides were desalted and concentrated using StageTip columns with C18 Empore disks (3M) inserted into 200-µL pipette tips. The columns were activated with 100 µL of 100% methanol and centrifuged for 2 minutes at 1,000 × g followed by equilibration with 100 µL of 0.1% formic acid under the same centrifugation conditions. Next, 200 µL of the samples were loaded onto the column and centrifuged until complete passage. Finally, the columns were twice with 200 µL of 0.1% formic acid. ["],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Mass spectrometry. The analysis was performed using an Ultimate 3000 nanoLC system (Thermo Fisher Scientific Inc.). Previously desalted peptides were analyzed in technical duplicates and loaded onto reverse-phase columns (30 cm length, 75 μm inner diameter) packed with ReproSil-Pur C18-AQ resin (Dr. Maisch; 3 μm particles; 120 Å pore size). Peptides were separated using a 120-min gradient, ranging from 5% to 40% mobile phase B (95% acetonitrile with 0.1% formic acid). The eluate was directly introduced into Orbitrap Fusion Lumos mass spectrometer (Thermo Fisher Scientific Inc.). Mass spectra were acquired on the Orbitrap Fusion Lumos in data-dependent acquisition (DDA) mode, automatically alternating between full MS and MS/MS scans, with a dynamic exclusion of 45 s. Full MS scans were acquired at a resolution of 60,000 (at m/z 200), with a cycle time of 2 s. The most intense ions with charge states of 2+ and 3+ were isolated and fragmented by higher-energy collisional dissociation (HCD) using a normalized collision energy of 30%. The chromatographic gradient and instrument operations were controlled using Xcalibur 4 software (Thermo Fisher Scientific Inc.). Parameters included a spray voltage of 2.6 kV, a capillary temperature of 250 °C, no auxiliary or sheath gas flow, and automatic gain control (AGC) enabled. The S-lens RF level was set to 70%. For peptide spectral matching (PSM) and PSM validation, data analysis was performed using the PatternLab for Proteomics V software (available at: http://www.patternlabforproteomics.org/ )(23). Peptide-Spectrum Matches (PSMs) were obtained using the Y.A.D.A. 3.0 algorithm, which identifies multiplexed MS2 spectra (24). At this stage, organism-specific protein databases were imported into the software. For C. deuterogattii R265, the database was retrieved from the FungiDB (available at https://fungidb.org/fungidb/app ) on October 10, 2025, corresponding to C. gattii VGII R265. For C. auris MMC2 (proteome ID: UP000230249) and C. parapsilosis GA1 (proteome ID: UP000005221), the protein dataset was obtained from UniProt (http://www.uniprot.org/) on October 25, 2025. PSM validation and filtering were performed using the Search Engine Processor (SEPro) and protein quantification was performed using extracted ion chromatograms (XIC). Only proteins identified with at least two unique peptides were retained, and contaminants and decoys entries were removed."],"omics_type":["Proteomics"],"labhead":["Marcio L. Rodrigues"],"instrument_platform":[""],"labhead_affiliation":["Instituto Carlos Chagas, Fundação Oswaldo Cruz (Fiocruz), Curitiba, Brazil"],"submission_type":["PARTIAL"],"species":["Cryptococcus Neoformans Rct29"],"publication":["42307779 Jozefowicz LJ, Bezerra BT, Veres E, Szilovics Z, Souza CM, Camillo-Andrade AC, Santos HGG, Carvalho PC, Santos MDM, Reis FCG, Gacser A, Rodrigues ML. Fungal Extracellular Vesicles are Recoverable Across Variable Ultracentrifugation Speeds but Display Species-specific Profiles of Sedimentation. J Membr Biol. 2026 259(1):21 10.1007/s00232-026-00386-3"],"submitter_mail":["marlondms@gmail.com"],"submitter_affiliation":["Computational Mass Spectrometry & Proteomics Group - Fiocruz"],"submitter_country":["Brazil"],"pubmed_abstract":["Extracellular vesicles (EVs) are central components of fungal biology, yet their isolation commonly relies on ultracentrifugation protocols originally developed for mammalian systems. In Cryptococcus, most EVs carry the capsular polysaccharide glucuronoxylomannan (GXM), raising the possibility that vesicle density, and therefore sedimentation, could be influenced by polysaccharide content. Here, we systematically evaluated EV recovery across sequential ultracentrifugation speeds (20,000 × g to 100,000 × g) in Cryptococcus deuterogattii, Candida auris, and Candida parapsilosis. In C. deuterogattii, GXM was detected across all ultracentrifugation fractions, and each fraction efficiently transferred polysaccharide to acapsular cells, demonstrating that its presence is independent of fraction density and does not correlate with sedimentation behavior. In the three fungal species, transmission electron microscopy and nanoparticle tracking analysis confirmed that bona fide EVs are recoverable across all centrifugation speeds. Qualitative and quantitative proteomic analyses revealed largely overlapping protein compositions among fractions within each species. However, proteomic profiles differed between species. In C. deuterogattii and C. auris, fractions displayed similar proteomic and predicted protein-protein interaction signatures across centrifugation speeds. In contrast, C. parapsilosis exhibited a clear partitioning pattern, with low-speed fractions (20,000 × g and 40,000 × g) clustering together and differing from higher-speed fractions (60,000-100,000 × g). These findings demonstrate that fungal EVs are recoverable across a broad range of ultracentrifugation speeds, but their sedimentation behavior is species-specific. Our study highlights the need for tailored EV isolation strategies and cautions against assuming methodological equivalence across fungal pathogens."],"pubmed_title":["Fungal Extracellular Vesicles are Recoverable Across Variable Ultracentrifugation Speeds but Display Species-specific Profiles of Sedimentation."],"pubmed_authors":["Jozefowicz Luisa J LJ, Bezerra Bárbara T BT, Veres Eva E, Szilovics Zóra Z, Souza Cássia M CM, Camillo-Andrade Amanda C AC, Santos Hellen G G HGG, Carvalho Paulo C PC, Santos Marlon D M MDM, Reis Flavia C G FCG, Gacser Attila A, Rodrigues Marcio L ML"],"additional_accession":[]},"is_claimable":false,"name":"Fungal extracellular vesicles are recoverable across variable ultracentrifugation speeds but display species-specific profiles of sedimentation","description":"Extracellular vesicles (EVs) are central components of fungal biology, yet their isolation commonly relies on ultracentrifugation schemes originally developed for mammalian systems. In Cryptococcus, most EVs carry the capsular polysaccharide glucuronoxylomannan (GXM), raising the possibility that vesicle density, and therefore sedimentation, could be influenced by polysaccharide content. Here, we systematically evaluated EV recovery across sequential ultracentrifugation speeds (20,000 × g to 100,000 × g) in Cryptococcus deuterogattii, Candida auris, and Candida parapsilosis. In C. deuterogattii, GXM was detected across all ultracentrifugation fractions, and each fraction efficiently transferred polysaccharide to acapsular cells, demonstrating that its presence is independent of fraction density and does not correlate with sedimentation behavior. In the three fungal species, transmission electron microscopy and nanoparticle tracking analysis confirmed that bona fide EVs are recoverable across all centrifugation speeds, with comparable size distributions. Qualitative and quantitative proteomic analyses revealed largely overlapping protein compositions among fractions within each species. However, proteomic profiles differed between species. In C. deuterogattii and C. auris, fractions displayed similar proteomic and predicted protein-protein interaction signatures across centrifugation speeds. In contrast, C. parapsilosis exhibited a clear partitioning pattern, with low-speed fractions (20,000 × g and 40,000 × g) clustering together and differing from higher-speed fractions (60,000–100,000 × g). These findings demonstrate that fungal EVs are recoverable across a broad range of ultracentrifugation speeds, but their sedimentation behavior is species-specific. Our study highlights the need for tailored EV isolation strategies and cautions against assuming methodological equivalence across fungal pathogens.","dates":{"publication":"2026-06-29","submission":"2026-03-31"},"accession":"PXD076414","cross_references":{"TAXONOMY":["NEWT:68239","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:44270","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:2433","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:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","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:1410384","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:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:467144","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:2423","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:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","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:1325292","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:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:941638","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:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:9938","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:483179","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:11294","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:487521","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT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