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Identification of overexpressed proteins under oxidative stress conditions in Candida auris

ABSTRACT: 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).

INSTRUMENT(S):

ORGANISM(S): Fungi [candida] Auris

SUBMITTER: Aitziber Antoran

LAB HEAD: Andoni Ramirez

PROVIDER: PXD051894 | Pride | 2025-10-23

REPOSITORIES: Pride

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			Action	DRS
	ANDONI_LEIRE_1_20220215_001.msf	Msf
	ANDONI_LEIRE_1_20220215_001.raw	Raw
	ANDONI_RAMIREZ_10_20221028_001.msf	Msf
	ANDONI_RAMIREZ_10_20221028_001.raw	Raw
	ANDONI_RAMIREZ_11_20221028_001.msf	Msf

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Project description:Data analysis. Spot detection and matching were performed with a comparative cross analysis of all the gels using DeCyder software v.6.5 (GE Healthcare). 178 spots were selected based on 1.15-fold for protein ratio cut-off, allowing for the appearance of the spots in 23 out of 28 gels (69 out of 84 total images). Data from 95 spots were submitted. 93 spots were identified with high confidence. Spot picking and Trypsin digestion. The spots of interest were picked up by Ettan Spot Picker (GE Healthcare) based on the in-gel analysis and spot picking design by DeCyder software. The gel spots were washed a few times then digested in-gel with modified porcine trypsin protease (Promega, Fitchburg, WI). The digested tryptic peptides were desalted using a Zip-tip C18 (Millipore, Billerica, MA). Peptides were eluted from the Zip-tip with 0.5 uL of matrix solution (alpha-cyano-4-hydroxycinnamic acid, 5 mg/mL in 50% acetonitrile, 0.1% trifluoroacetic acid, 25mM ammonium bicarbonate) and spotted on a MALDI plate. Mass Spectrometry. MALDI-TOF MS and TOF/TOF tandem MS/MS were performed on AB SCIEX TOF/TOF 5800 System (AB SCIEX). MALDI-TOF mass spectra were acquired in reflectron positive ion mode, averaging 4000 laser shots per spectrum. TOF/TOF tandem MS fragmentation spectra were acquired for each sample, averaging 4000 laser shots per fragmentation spectrum on each of the 7-10 most abundant ions present in each sample (excluding trypsin autolytic peptides and other known background ions). Database search. Both the resulting peptide mass and the associated fragmentation spectra were submitted to GPS Explorer workstation equipped with MASCOT search engine (Matrix Science, Boston, MA) to search the Swiss-Prot database. Searches were performed without constraining protein molecular weight or isoelectric point, with variable carbamidomethylation of cysteine and oxidation of methionine residues, and with one missed cleavage also allowed in the search parameters. Candidates with either protein score C.I.% or Ion C.I.% greater than 95 were considered significant. When multiple IDs were significant for a given spot, the selection was made by evaluating apparent molecular weight, isoelectric point, the location of the spot in the gel, and the presence of strips of multiple protein isoforms in the adjacent spots.

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Identification of overexpressed proteins under oxidative stress conditions in Candida auris

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