PXD022623-1

PXD022623 is an original dataset announced via ProteomeXchange.

Title	Comparative proteomics of Histoplasma capsulatum
Description	Histoplasma capsulatum is a thermally dimorphic fungus with worldwide distribution, and high incidence in the Americas. It is the etiologic agent of histoplasmosis, an important life-threatening systemic mycosis. Dimorphism is an important feature for fungal survival in different environments and it has been related to the virulence of H. capsulatum, and essential to the establishment of infection. Proteomic profiles have brought important contributions to the knowledge of metabolism and pathogenicity in several biological models. However, studies of the H. capsulatum proteome have been underexplored. In the present study, we report the first proteomic comparison between the mycelium and the yeast cells of H. capsulatum. Liquid chromatography coupled to mass spectrometry was used to evaluate the proteomic profile of the two phases of H. capsulatum. In summary, 214 proteins were only detected/or preferentially abundant in mycelium, while the same occurred to 335 proteins in yeast cells. In mycelium, enzymes related to the glycolytic pathway and to the alcoholic fermentation showed greater abundance, suggesting a higher use of anaerobic pathways for energy production. In yeast cells, proteins related to the tricarboxylic acid cycle and response to temperature stress showed high abundance. Proteins related to oxidative stress response or involved with cell wall metabolism were identified with differential abundance in both conditions. Validation of proteomic data was performed by enzymatic activity determination, western blot assays, or immunofluorescence microscopy. These experiments corroborated, directly or indirectly, the abundance of isocitrate lyase, 2-methylcitrate synthase, catalase B, and mannosyl-oligosaccharide-1,2-alpha-mannosidase in the mycelium and heat shock protein (HSP) 30, HSP60, glucosamine-fructose-6-phosphate aminotransferase, glucosamine-6-phosphate deaminase, and N-acetylglucosamine-phosphate mutase in yeast-cells. The proteomic profile associated functional classification analyzes of proteins provided a better understanding of the metabolic reorganization and cell wall remodeling on the yeast form of H. capsulatum.
HostingRepository	PRIDE
AnnounceDate	2021-09-09
AnnouncementXML	Submission_2021-09-09_14:13:05.021.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	CLAYTON BORGES
SpeciesList	scientific name: Histoplasma capsulatum; NCBI TaxID: 5037;
ModificationList	phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Synapt MS

Revision	Datetime	Status	ChangeLog Entry
0	2020-11-19 03:32:10	ID requested
⏵ 1	2021-09-09 14:13:05	announced

Almeida MA, Baeza LC, Almeida-Paes R, Bail, ã, o AM, Borges CL, Guimar, ã, es AJ, Soares CMA, Zancop, é, -Oliveira RM, Yeast and Mycelium Reveals Differential Metabolic Shifts and Cell Wall Remodeling Processes in the Different Morphotypes. Front Microbiol, 12():640931(2021) [pubmed]

submitter keyword: Histoplasma capsulatum, dimorphism, yeast, mycelium, proteomic analysis, fungal biology

CLAYTON LUIZ BORGES
contact affiliation	Federal University of Goias
contact email	clbluiz2@gmail.com
lab head
CLAYTON BORGES
contact affiliation	Biochemistry and molecular biology department, Universidade Federal de Goias, Brazil
contact email	clbluiz2@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD022623
     1. Label: PRIDE project
     2. Name: Comparative proteomics of Histoplasma capsulatum