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

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dc.contributor.author Ilyas, Sidra
dc.contributor.author Rehman, Abdul
dc.contributor.author Varela, Ana Coelho
dc.contributor.author Sheehan, David
dc.date.accessioned 2016-02-17T11:43:39Z
dc.date.available 2016-02-17T11:43:39Z
dc.date.issued 2014
dc.identifier.citation Ilyas 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.volume 9 en
dc.identifier.issued 7 en
dc.identifier.issn 1932-6203
dc.identifier.uri http://hdl.handle.net/10468/2330
dc.identifier.doi 10.1371/journal.pone.0102340
dc.description.abstract Trichosporon 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.sponsorship Higher Education Authority (Programme for Research in Third Level Institutions); Higher Education Commission, Pakistan (International Research Initiative Programme) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher Public Library of Science en
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 credited en
dc.rights.uri http://creativecommons.org/licenses/by/4.0/ en
dc.subject Reversible cysteine oxidation en
dc.subject Rhodotorula sp Y11 en
dc.subject Saccharomyces cerevisiae en
dc.subject Two-dimensional electrophoresis en
dc.subject Hydrogen peroxide en
dc.subject Genome sequence en
dc.subject Heavy metals en
dc.subject In vivo en
dc.subject Cadmium en
dc.subject Yeast en
dc.title 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 en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother David Sheehan, School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: d.sheehan@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.internal.wokid WOS:000339992600012
dc.contributor.funder Higher Education Authority
dc.contributor.funder Higher Education Commission, Pakistan
dc.description.status Peer reviewed en
dc.identifier.journaltitle PLOS ONE en
dc.internal.IRISemailaddress d.sheehan@ucc.ie en
dc.identifier.articleid e102340


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© 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 credited Except where otherwise noted, this item's license is described as © 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 credited
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