Redox proteomics changes in the fungal pathogen Trichosporon asahii on arsenic exposure: identification of protein responses to metal-induced oxidative stress in an environmentally-sampled isolate

dc.contributor.authorIlyas, Sidra
dc.contributor.authorRehman, Abdul
dc.contributor.authorVarela, Ana Coelho
dc.contributor.authorSheehan, David
dc.contributor.funderHigher Education Authority
dc.contributor.funderHigher Education Commission, Pakistan
dc.description.abstractTrichosporon asahii is a yeast pathogen implicated in opportunistic infections. Cultures of an isolate collected from industrial wastewater were exposed for 2 days to 100 mg/L sodium arsenite (NaAsO2) and cadmium (CdCl2). Both metals reduced glutathione transferase (GST) activity but had no effect on superoxide dismutase or catalase. NaAsO2 exposure increased glutathione reductase activity while CdCl2 had no effect. Protein thiols were labeled with 5-iodoacetamido fluorescein followed by one dimensional electrophoresis which revealed extensive protein thiol oxidation in response to CdCl2 treatment but thiol reduction in response to NaAsO2. Two dimensional electrophoresis analyses showed that the intensity of some protein spots was enhanced on treatment as judged by SameSpots image analysis software. In addition, some spots showed decreased IAF fluorescence suggesting thiol oxidation. Selected spots were excised and tryptic digested for identification by MALDI-TOF/TOF MS. Twenty unique T. asahii proteins were identified of which the following proteins were up-regulated in response to NaAsO2: 3-isopropylmalate dehydrogenase, phospholipase B, alanine-glyoxylate aminotransferase, ATP synthase alpha chain, 20S proteasome beta-type subunit Pre3p and the hypothetical proteins A1Q1_08001, A1Q2_03020, A1Q1_06950, A1Q1_06913. In addition, the following showed decreased thiol-associated fluorescence consistent with thiol oxidation; aconitase; aldehyde reductase I; phosphoglycerate kinase; translation elongation factor 2; heat shock protein 70 and hypothetical protein A1Q2_04745. Some proteins showed both increase in abundance coupled with decrease in IAF fluorescence; 3-hydroxyisobutyryl-CoA hydrolase; homoserine dehydrogenase Hom6 and hypothetical proteins A1Q2_03020 and A1Q1_00754. Targets implicated in redox response included 10 unique metabolic enzymes, heat shock proteins, a component of the 20S proteasome and translation elongation factor 2. These data suggest extensive proteomic alterations in response to metal-induced oxidative stress in T. asahii. Amino acid metabolism, protein folding and degradation are principally affected.en
dc.description.sponsorshipHigher Education Authority (Programme for Research in Third Level Institutions); Higher Education Commission, Pakistan (International Research Initiative Programme)en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.identifier.citationIlyas S, Rehman A, Varela AC, Sheehan D (2014) Redox Proteomics Changes in the Fungal Pathogen Trichosporon asahii on Arsenic Exposure: Identification of Protein Responses to Metal-Induced Oxidative Stress in an Environmentally-Sampled Isolate. PLoS ONE 9(7): e102340. doi:10.1371/journal.pone.0102340
dc.identifier.journaltitlePLOS ONEen
dc.publisherPublic Library of Scienceen
dc.rights© 2015 Ilyas et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are crediteden
dc.subjectReversible cysteine oxidationen
dc.subjectRhodotorula sp Y11en
dc.subjectSaccharomyces cerevisiaeen
dc.subjectTwo-dimensional electrophoresisen
dc.subjectHydrogen peroxideen
dc.subjectGenome sequenceen
dc.subjectHeavy metalsen
dc.subjectIn vivoen
dc.titleRedox proteomics changes in the fungal pathogen Trichosporon asahii on arsenic exposure: identification of protein responses to metal-induced oxidative stress in an environmentally-sampled isolateen
dc.typeArticle (peer-reviewed)en
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