PXD057826

PXD057826 is an original dataset announced via ProteomeXchange.

Title	Potential Role of Lysine Acetylation in the Stepwise Adaptation of Candida albicans to Fluconazole
Description	Candida albicans is an opportunistic fungal pathogen capable of causing superficial mucosal and systemic infections, sometimes leading to life-threatening conditions. The increasing resistance of C. albicans to azole antifungals has become a significant challenge in clinical treatment. Lysine acetylation (Kac) is a well-studied post-translational modification that plays crucial roles in various biological processes. However, its impact on antifungal resistance in C. albicans remains poorly understood. Five strains of C. albicans isolated from the same patient, representing different stages of acquired fluconazole resistance in vivo, were used in this study to investigate the potential regulatory mechanism of Kac on the development of azole resistance in C. albicans. Quantitative proteomic analysis using tandem mass tag (TMT) labeling, acetylation enrichment, and liquid chromatography-mass spectrometry (LC-MS) was conducted on these five strains. We divided all strains into four comparison groups and identified a total of 1796 lysine acetylation sites across 938 proteins, with quantitative data available for 1314 acetylation sites in 712 proteins. Analysis of 155 significantly differentially modified sites revealed that the acetylation levels of key proteins involved in the conversion of pyruvate to acetyl-CoA for entry into the tricarboxylic acid (TCA) cycle for energy production were initially downregulated and then upregulated during the acquisition of fluconazole resistance. Additionally, the acetylation levels of proteins involved in ribosome synthesis, translation processes, and amino acid synthesis were found to increase. Therefore, lysine acetylation in C. albicans may contribute to azole resistance by regulating energy metabolism and protein synthesis.
HostingRepository	PRIDE
AnnounceDate	2025-03-25
AnnouncementXML	Submission_2025-03-25_05:53:53.250.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nana Song
SpeciesList	scientific name: Candida albicans (Yeast); NCBI TaxID: 5476;
ModificationList	acetylated residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2024-11-12 21:44:42	ID requested
⏵ 1	2025-03-25 05:53:53	announced

10.1128/SPECTRUM.02797-24;

submitter keyword: Candida albicans

acquired fluconazole resistance in vivo

lysine acetylation

tandem mass tag labeling

Nana Song
contact affiliation	Department of Medical Mycology, Hospital for Skin Diseases, Institute of Dermatology, Chinese Academy of Medical Sciences and Peking Union Medical College
contact email	nanas25@foxmail.com
lab head
Nana Song
contact affiliation	Department of Medical Mycology, Institute of Dermatology, Chinese Academy of Medical Sciences and Peking Union Medical College
contact email	nanas25@foxmail.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/2025/03/PXD057826

PRIDE project URI

• PRIDE
  1. PXD057826
     1. Label: PRIDE project
     2. Name: Potential Role of Lysine Acetylation in the Stepwise Adaptation of Candida albicans to Fluconazole