PXD066550

PXD066550 is an original dataset announced via ProteomeXchange.

Dataset Summary

Title	An anti-adhesive peptide found in extracellular vesicles from Sporothrix brasiliensis and Sporothrix schenckii
Description	Background Sporothrix brasiliensis and Sporothrix schenckii are the main etiological agents of sporotrichosis. These pathogens release extracellular vesicles (EVs), which are key transport structures involved in virulence and host–pathogen interactions. EVs from S. brasiliensis and S. schenckii have been exclusively under liquid culture conditions, with analyses focused on their protein composition and functional roles. However, noinformation is currently available regarding the small molecule composition of Sporothrix EVs, and the extent to wich S. schenckii and S. brasiliensis share or differ in their EVs cargo remain unknown. Methods We isolated EVs from S. brasiliensis (strain 5110) and S. schenckii (strain 1099-18) following cultivation on solid medium, and characterized the samples using a combination of nanoparticle tracking analysis (NTA), transmission electron microscopy (TEM), proteomics, and small molecule identification. Based on the EV composition, subsequent analyses included biochemical assay to assess cell-assocaited enzyme activity and a functional model of Sporothrix adhesion to type I collagen in the presence of isoleucine-proline-isoleucine (IPI), a peptide component found in EVs produced by both S. schenckii and S. brasiliensis. Results EVs from both S. brasiliensis and S. schenckii exhibited a high protein diversity, encompassing components related to essential cellular processes and virulence mechanisms. Only a small fraction of the identified proteins was shared between the two species, and a similar pattern was observed for the small molecules. Among the common molecules was IPI, previously described in Cryptococcus EVs. IPI is an inhibitor of dipeptidyl peptidase IV (DPP4), which was detected on the surface of S. brasiliensis and S. schenckii. Both IPI and an antibody against DPP4 effectively reduced Sporothrix adhesion to type I collagen, a major component of the host extracellular matrix. Conclusion Our study reveals an unprecedented level of proteomic and metabolomic complexity in Sporothrix EVs, uncovering novel molecular features and identifying IPI as an inhibitor of fungal adhesion to collagen.
HostingRepository	PRIDE
AnnounceDate	2025-09-15
AnnouncementXML	Submission_2025-09-14_16:24:37.556.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Marlon D M Santos
SpeciesList	scientific name: Sporothrix sp.; NCBI TaxID: 1902615;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Exploris 480

Dataset History

Revision	Datetime	Status	ChangeLog Entry
0	2025-07-24 09:27:34	ID requested
⏵ 1	2025-09-14 16:24:38	announced

Publication List

10.1038/s41467-025-63442-x;
Orth B, Pohl P, Aust F, Ji Y, Seenivasan A, Dybkov O, Liang XJ, Bock L, Leidner F, Levantovsky S, Schardey P, Sander P, Disch NJ, Trautz ML, Mizi A, Papantonis A, Lenz C, Grubm, ü, ller H, Steinchen W, Behrends C, Urlaub H, Gehringer M, Lorenz S, Selective ubiquitination of drug-like small molecules by the ubiquitin ligase HUWE1. Nat Commun, 16(1):8182(2025) [pubmed]

10.1038/s41467-025-63442-x;

Orth B, Pohl P, Aust F, Ji Y, Seenivasan A, Dybkov O, Liang XJ, Bock L, Leidner F, Levantovsky S, Schardey P, Sander P, Disch NJ, Trautz ML, Mizi A, Papantonis A, Lenz C, Grubm, ü, ller H, Steinchen W, Behrends C, Urlaub H, Gehringer M, Lorenz S, Selective ubiquitination of drug-like small molecules by the ubiquitin ligase HUWE1. Nat Commun, 16(1):8182(2025) [pubmed]

Keyword List

submitter keyword: small molecules, Sporothrix,Extracellular vesicles, adhesion, proteome

submitter keyword: small molecules, Sporothrix,Extracellular vesicles, adhesion, proteome

Contact List

Marcio L. Rodrigues
contact affiliation	Instituto Carlos Chagas, Fundação Oswaldo Cruz (Fiocruz), Curitiba, Brazil,
contact email	marcio.rodrigues@fiocruz.br
lab head
Marlon D M Santos
contact affiliation	Computational Mass Spectrometry & Proteomics Group - Fiocruz
contact email	marlondms@gmail.com
dataset submitter

Full Dataset Link List

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PRIDE project URI

Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/09/PXD066550

PRIDE project URI

Repository Record List

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