PXD056961

PXD056961 is an original dataset announced via ProteomeXchange.

Title	Proteomic studies on the effects of the deletion of two aminophospholipid translocases in the cellular and extracellular vesicle fractions of Cryptococcus neoformans
Description	Flippases are enzymes responsible for the architecture of eukaryotic membranes, regulating various mechanisms of molecular transport and lipid translocation. In Cryptococcus neoformans, a major fungal pathogen, the aminophospholipid translocase 1 (Apt1) flippase plays roles in fungal virulence, membrane architecture, and extracellular vesicle (EV) polysaccharide cargo, among other physiological processes, making this enzyme a potential drug target. The effect of APT1 deletion on the fungal proteome is unknown, limiting the understanding of how this enzyme functions in cryptococcal physiology. The APT gene family includes other members, such as APT2, whose functions in C. neoformans are virtually unknown. In this study, we first investigated the impact of APT1 and APT2 deletion on EV formation in C. neoformans. We found that EV formation was not quantitatively affected by the deletion of APT1 or APT2. As previously observed, the absence of Apt1 resulted in decreased polysaccharide concentration in EVs, but the deletion of APT2 did not affect vesicular polysaccharide concentration. To gain a deeper understanding of how Apt1 and Apt2 influence the physiology of C. neoformans, we then characterized the EV and cellular proteomes of C. neoformans mutants lacking expression of the APT1 and APT2 genes, comparing them to the proteomes of wild-type (WT) cells. Our results show that the deletion of APT1 and APT2 impacts both the cellular and EV proteomes of C. neoformans, with unique elements related to each gene. These findings demonstrate the differential roles of Apt1 and Apt2 in EV formation and suggest their direct involvement in the physiology of C. neoformans. Our results contribute to the understanding of how cryptococcal flippases could be targeted by drugs in the future.
HostingRepository	PRIDE
AnnounceDate	2026-06-29
AnnouncementXML	Submission_2026-06-28_16:36:55.508.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Marlon D M Santos
SpeciesList	scientific name: Cryptococcus neoformans Tu401-MP_1; NCBI TaxID: NEWT:1202389;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2024-10-18 20:00:15	ID requested
⏵ 1	2026-06-28 16:36:56	announced

Castelli RF, de Oliveira HC, Santos MDM, Camillo-Andrade AC, Dos Reis FCG, Carvalho PC, Rodrigues ML, The flippases Apt1 and Apt2 differentially influence extracellular vesicle cargo and polysaccharide secretion in Cryptococcus neoformans. J Proteomics, 319():105483(2025) [pubmed]

10.1016/j.jprot.2025.105483;

submitter keyword: Proteomic;deletiontranslocases;cellular;extracellular vesicle;Cryptococcus neoformans

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

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/2026/06/PXD056961

PRIDE project URI

• PRIDE
  1. PXD056961
     1. Label: PRIDE project
     2. Name: Proteomic studies on the effects of the deletion of two aminophospholipid translocases in the cellular and extracellular vesicle fractions of Cryptococcus neoformans