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Secretome of Candidozyma auris at pH 5.5 and pH 7.5

ABSTRACT: In this work, we used high-throughput mass-spectroscopy analysis to identify polypeptides secreted by C. auris into growth medium at two different physiological pH conditions: pH 5.5 and pH 7.5.

INSTRUMENT(S):

ORGANISM(S): Candidozyma Aff. Auris

TISSUE(S): Blood

SUBMITTER: Vladimir Kaberdin

LAB HEAD: Vladimir Kaberdin

PROVIDER: PXD060071 | Pride | 2026-05-27

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	C.aurisResults.mzTab	Mztab
	C.aurispH5.5.R1.raw	Raw
	C.aurispH5.5.R2.raw	Raw
	C.aurispH5.5.R3.raw	Raw
	C.aurispH7.5.R1.raw	Raw

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Project description:The goal of this work was to compare strains from the C. auris clades by assessing some virulence factor, such as cell surface hydrophobicity and biofilm formation. Our results indicate key phenotypic differences between strains assigned to different C. auris clades, which were validated by the use of C. auris ALS and IFF mutants (knocked out or reconstituted).

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Candida auris proteomic profiling

Project description:In this study, we designed a novel antifungal agent, PQA-Az-13 that demonstrated antifungal activity against C. auris biofilms. Cellular proteomics indicated that PQA-Az-13 partially or completely inhibited numerous enzymatic proteins in C. auris biofilms, particularly those involved in both amino acid biosynthesis and metabolism processes, as well as in general energy-producing processes. Due to its hydrophobic nature and limited aqueous solubility, PQA-Az-13 was encapsulated in cationic liposomes and characterized by biophysical and spectral techniques. PQA-Az-13 liposomes demonstrated enhanced antifungal activity levels against both C. auris in in vitro biofilms and ex vivo skin colonization models.

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Evaluation of Ca37 monoclonal antibody against pathogenic fungal Candidozyma auris

Project description:Candidozyma auris, previously known as Candida auris, is a recently found pathogenic yeast that causes systemic infections, showing a high mortality rate. Moreover, this species is highly resistant to the commonly used antifungal drugs and some of the strains are multiresistant. This fungus is also able to cause outbreaks in hospital settings. All of this has cause an alarm in the health care system. Therefore, finding alternative treatments for C. auris is critical. In this sense, our research group developed a monoclonal antibody (Ca37) against Candida albicans alcohol dehydrogenase enzyme (Adh) that successfully reduced the growth of the fungus in vitro and also showed a protective effect in vivo. Due to the high homology between both fungal alcohol dehydrogenases, we wanted to test the effect of Ca37 over C. auris. In order to do this, first we assessed if the monoclonal antibody also recognized C. auris Adh by sequencing the spots detected by two dimensional western blot when using the monoclonal antibody as first antibody. Two spots were detected in this western blot. The sequencing showed a mixture of proteins, but in both cases, Adh was one of the identified proteins.

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A single gene mutation underpins metabolic adaptation and acquisition of filamentous competence in the emerging fungal pathogen Candida auris

Project description:Filamentous cell growth is a vital property of fungal pathogens. The mechanisms of filamentation in the emerging multidrug-resistant fungal pathogen Candida auris are poorly understood. Here, we show that exposure of C. auris to glycerol triggers a rod-like filamentation-competent (RL-FC) phenotype, which forms elongated filamentous cells after a prolonged culture period. Whole-genome sequencing analysis reveals that all RL-FC isolates harbor a mutation in the C2H2 zinc finger transcription factor-encoding gene GFC1 (Gfc1 variants). Deletion of GFC1 leads to an RL-FC phenotype similar to that observed in Gfc1 variants. We further demonstrate that GFC1 mutation causes enhanced fatty acid β-oxidation metabolism and thereby promotes RL-FC/filamentous growth. This regulation is achieved through a Multiple Carbon source Utilizer (Mcu1)-dependent mechanism. Interestingly, both the evolved RL-FC isolates and the gfc1Δ mutant exhibit an enhanced ability to colonize the skin. Our results reveal that glycerol-mediated GFC1 mutations are beneficial during C. auris skin colonization and infection.

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Project description:Candida auris is a recently found pathogenic yeast that causes systemic infections, showing a high mortality rate. In addition, C. auris has been found to be difficult to remove from the environment of health care settings, among other causes due to its high resistance to stress conditions. Moreover, the reactive oxygen species that cause the oxidative stress are also used by our immune cells to kill the microorganisms. Considering this, our research group has studied the proteomic changes that are associated to the presence of high oxidative stress conditions (8 mM H2O2) in the fungus C. auris. Thirteen spots were found to be overexpressed between normal and oxidative stress conditions; four were specific points only detected under oxidative stress and nine were overexpressed in this condition. Fifteen proteins were identified in this spots. The four spots detected as specifically expressed corresponded to the proteins ubiquitin-activating enzyme e1 (Uba1), elongation factor 3 (Cef3), leucine—tRNA ligase (Cdc60), an uncharacterized protein (A0A2H0ZCS4), and thioredoxin-dependent peroxiredoxin (Tsa1b). The uncharacterized protein had the same amino acid sequence as the formyltetrahydrofolate synthetase (Fau1) found in another C. auris strain. On the other hand, the nine spots detected as overexpressed corresponded to the proteins mitochondrial C-1-tetrahydrofolate (Mis1), Fau1, 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase (Met6), 40S ribosomal protein S6 (Rps6), 60S ribosomal protein L8 (Rpl8), 40S ribosomal protein S4 (Rps4), elongation factor 1-α (Tef1), ATP synthase subunit β (Atp2), acetyl-CoA C-acetyltransferase (Erg10), mitochondrial aconitate hydratase (Aco1) and malate dehydrogenase (Mdh1).

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