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Protein composition was determined in  both cellular extracts and EV samples. EVs were isolated as previously described (53). For extraction three independent biological replicates of C. neoformans (WT and dpp4 strains) were pre-cultured in Sabouraud’s liquid medium overnight at 30oC with agitation (200 rpm). The next day, inocula of 106 cells/mL were prepared in Sabouraud broth and incubated for 24 h with agitation (200 rpm) at 30 or 37oC. After incubation, the cells were washed three times with PBS and the pellets were immediately frozen in an ultra-freezer (–80 °C) and, once frozen, subjected to lyophilization under pressure conditions at 0.04 mBar and a temperature of –50 °C for 18 h. EV and cell lysis were then performed by adding 0.1 mm zirconium beads to the dried pellets and subjecting them to 10 cycles of vortexing for 1 min, each followed by 1 min of incubation on ice. Subsequently, 100 µL of 8 M urea was added to each sample, and the lysis procedure was repeated for an additional five cycles under the same conditions. Lysates were centrifuged at 18,000 x g for 15 min at 4°C, as previously described (54). Supernatants were collected, and protein concentrations were determined by fluorometric quantification using a Qubit fluorometer (Thermo Fisher Scientific Inc.). One hundred µg of protein from each sample were reduced with dithiothreitol (DTT) to a final concentration of 10 mM for 30 min at 60 °C. After cooling to room temperature, samples were alkylated with iodoacetamide (IAA) to a final concentration of 30 mM for 25 min at room temperature in the dark. Excess IAA was quenched by a second incubation with DTT (final concentration of 5 mM) for 15 min at room temperature. Proteins were then digested overnight with trypsin at an enzyme-to-substrate ratio of 1:50. The resulting peptides were desalted and concentrated using Stage-Tips, as described by Rappsilber et al. (55). Peptide concentrations were determined by fluorometric assay using a Qubit fluorometer, following the manufacturer’s instructions.Mass spectrometry. In technical duplicates, desalted peptides were loaded onto in-house packed reversed-phase columns containing Reprosil-Pur C18 Aqua stationary phase (3 µm particle size, 120 Å pore size; Dr. Maisch). The columns were 30 cm in length and had an internal diameter of 75 µm. Peptide loading and separation were performed using an Ultimate 3000 nano-liquid chromatography system (Thermo Fisher Scientific Inc.). Peptides were eluted using a 120-min linear gradient, increasing from 5% to 40% of mobile phase B, composed of 95% acetonitrile in 0.1% formic acid. The eluate was directly introduced into an Orbitrap Fusion Lumos mass spectrometer (Thermo Fisher Scientific Inc.) installed at the Proteomics and Mass Spectrometry Facility of the Carlos Chagas Institute (Fiocruz-PR). Mass spectrometric data were acquired in data-dependent acquisition (DDA) mode, with automatic alternation between full MS and MS/MS scans and a dynamic exclusion window of 60 s. Full MS scans were acquired at a resolution of 60,000 at m/z 200. Within a 2 s cycle time, the most intense precursor ions were selected for fragmentation, excluding unassigned ions and those with a +1 charge state. Selected ions were sequentially isolated and fragmented by higher-energy collisional dissociation (HCD) using a normalized collision energy of 30. Fragment ions were analyzed at a resolution of 15,000 at m/z 200."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peptide spectral matching (PSM) and PSM validation. Peptide spectral matching (PSM) and subsequent validation were performed using modules from the PatternLab for Proteomics V software suite (http://www.patternlabforproteomics.org/), employing the multiplexed spectra identification feature based on the YADA 3.0 deconvolution algorithm; this allows for the identification of more than one peptide per mass spectrum. A target–decoy database was constructed to ensure reliable identifications and consisted of Cryptococcus neoformans protein sequences retrieved from UniProt on November 1, 2025, including the reversed sequence of each entry, as well as 127 common mass spectrometry contaminants (e.g., keratin and trypsin). Tandem mass spectra were searched against this database using the Comet search engine. Searches were restricted to tryptic peptides allowing up to two missed cleavages, with carbamidomethylation of cysteine defined as a fixed modification and oxidation of methionine as a variable modification. PSM validation was carried out using the Search Engine Processor (SEPro). Identifications were grouped according to charge state (+2 and ≥+3), and Comet-derived parameters, including cross-correlation (XCorr), DeltaCN, and spectrum count score, were combined to generate a Bayesian discriminator. PSMs were ranked based on discriminator values, and cutoff thresholds were established to achieve a 1% false discovery rate (FDR) at the protein level, as estimated by the number of labeled decoy hits. Only peptide sequences containing six or more amino acid residues were considered. Additional post-processing filters were applied to retain PSMs with a mass error below 6 ppm, a minimum XCorr value of 2.0, and proteins supported by at least one independent piece of evidence. These criteria ensured that the final dataset met a global protein-level FDR of 1%."],"omics_type":["Proteomics"],"labhead":["Marcio L."],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Instituto Carlos Chagas, Fundação Oswaldo Cruz (Fiocruz), Curitiba, Brazil"],"species":["Cryptococcus Neoformans"],"publication":["Not available"],"submitter_mail":["marlondms@gmail.com"],"submitter_affiliation":["Computational Mass Spectrometry & Proteomics Group - Fiocruz"],"submitter_country":["Brazil"],"additional_accession":[]},"is_claimable":false,"name":"Dipeptidyl peptidase IV contributes to the pathogenesis of Cryptococcus neoformans","description":"We previously identified isoleucine–proline–isoleucine (IPI) as a small molecule associated with extracellular vesicles (EVs) in Cryptococcus. The administration of IPI controlled experimental cryptococcal infection through mechanisms that remain unknown. IPI is an inhibitor of dipeptidyl peptidase 4 (DPP4), an enzyme that regulates insulin and glucose homeostasis in mammals and may also influence pathogenic processes in fungi. Based on these observations, we investigated the biological and pathogenic roles of cryptococcal DPP4. We demonstrate that Cryptococcus neoformans expresses an active, surface-associated DPP4 that is inhibited by IPI. Deletion of the DPP4-encoding gene (CNAG_06416) abolished DPP4 enzymatic activity and resulted in marked physiological alterations, including changes in the proteomic composition of whole cells and EVs, as well as increased accumulation of undivided cells at 37°C both in vitro and in vivo. The dpp4Δ mutant was less lethal than wild-type (WT) cells in a Galleria mellonella infection model. In contrast, increased DPP4 activity did not enhance lethality, as demonstrated by the ability of WT and 19 high–DPP4-expressing mutant strains to kill G. mellonella. In a murine model, loss of DPP4 significantly attenuated fungal virulence, delaying host mortality and reducing fungal burden, particularly in the brain. This finding is consistent with the observation that dpp4Δ cells were markedly less efficient at crossing endothelial and extracellular matrix layers than WT cells. Collectively, these findings establish DPP4 as an important regulator of cryptococcal physiology and pathogenesis, and support the concept that targeting DPP4 may offer translational opportunities distinct from conventional antifungal 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