Proteomic analysis of cytosolic proteins associated with petite mutations in Candida glabrata

Penha, Carla V. Loureiro y; Kubitschek, P H B; Larcher, Gérald; Perales, Jonás; León, Ileana R.; Lópes-Bezerra, Leila M.; Bouchara, Jean‐Philippe

doi:10.1590/s0100-879x2010007500125

Cited by 7 publications

(4 citation statements)

References 36 publications

(31 reference statements)

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“…The exact mechanisms underlying fluconazole resistance are not well known. Recently, however, a proteomic analysis study revealed a series of proteins associated with antifungal agent resistance [16]. In this study, we determined that cellular and membrane proteins are differentially expressed between fluconazole-susceptible and -resistant strains.…”

Section: Discussionmentioning

confidence: 95%

Proteomic Analysis of Cellular and Membrane Proteins in Fluconazole-Resistant Candida glabrata

Yoo

Choi

Kim

et al. 2012

Osong Public Health and Research Perspectives

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ObjectivesCandida glabrata is one of the most common causes of Candida bloodstream infections worldwide. Some isolates of C glabrata may be intermediately resistant to azoles, with some strains developing resistance during therapy or prophylaxis with fluconazole. In this study, we used a proteomic approach to identify differentially expressed proteins between fluconazoleresistant and -susceptible strains.MethodsMembrane and cellular proteins were extracted from fluconazolesusceptible and fluconazole-resistant C glabrata strains. Differentially expressed proteins were compared using two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis. Proteins with >1.5-fold difference in expression were identified by liquid chromatography tandem mass spectrometry (LC-MS/MS).ResultsA total of 65 proteins were differentially expressed in the cellular and membrane fractions. Among the 39 cellular proteins, 11 were upregulated and 28 were downregulated in fluconazole-resistant strains in comparison with fluconazole-susceptible strains. In the membrane fraction, a total of 26 proteins were found, of which 19 were upregulated and seven were downregulated. A total of 31 proteins were identified by LC-MS/MS that are involved in glycolysis, carbohydrate transport, energy transfer, and other metabolic pathways. Heat shock proteins were identified in various spots.ConclusionHeat shock and stress response proteins were upregulated in the membrane fraction of the fluconazole-resistant C glabrata strain. Compared with susceptible strains, fluconazole-resistant strains showed increased expression of membrane proteins and decreased expression of cellular proteins.

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Section: Discussionmentioning

confidence: 95%

Proteomic Analysis of Cellular and Membrane Proteins in Fluconazole-Resistant Candida glabrata

Yoo

Choi

Kim

et al. 2012

Osong Public Health and Research Perspectives

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“…Alternatively, strain differences in Hst 5 uptake might be due to differing cellular requirements for polyamines related to intracellular polyamine stores or alternative biosynthesis. For example, the C. glabrata enzyme spermidine synthase SPE'3P: CAGL0D01408g is differentially expressed in azole resistant C. glabrata strains [40], [41]. More information is needed to identify and map the polyamine biosynthesis pathway in C. glabrata .…”

Section: Discussionmentioning

confidence: 99%

Histatin 5 Resistance of Candida glabrata Can Be Reversed by Insertion of Candida albicans Polyamine Transporter-Encoding Genes DUR3 and DUR31

Tati

Jang

et al. 2013

PLoS ONE

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Candida albicans and Candida glabrata are predominant fungi associated with oral candidiasis. Histatin 5 (Hst 5) is a small cationic human salivary peptide with high fungicidal activity against C. albicans, however many strains of C. glabrata are resistant. Since Hst 5 requires fungal binding to cell wall components prior to intracellular translocation, reduced Hst 5 binding to C. glabrata may be the reason for its insensitivity. C. glabrata has higher surface levels of β-1,3-glucans as compared with C. albicans; however these differences did not account for reduced Hst 5 uptake and killing in C. glabrata. Similarly, the biofilm matrix of C. glabrata contained significantly higher levels of β-1,3-glucans compared with C. albicans, but it did not reduce the percentage of Hst 5 positive fungal cells in the biofilm. Hst 5 enters C. albicans cell through polyamine transporters Dur3p and Dur31p that are uncharacterized in C. glabrata. C. glabrata strains expressing CaDur3 and CaDur31 had two-fold higher killing and uptake of Hst 5. Thus, neither C. glabrata cell surface or biofilm matrix β-1,3-glucan levels affected Hst 5 toxicity; rather the crucial rate limiting step is reduced uptake that can be overcome by expression of C. albicans Dur proteins in C. glabrata.

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“…Unfortunately, a handful of studies on C. glabrata azole-resistant isolates are missing specific gene identifying information, but similarly indicated by biological process data that proteins involved in glucose metabolism and cell wall biogenesis were differentially expressed in azole-resistant strains compared to azole-sensitive cells (Loureiro Y Penha et al . 2010 ; Yoo et al . 2012 , 2013 ).…”

Section: Transcriptomics Proteomics and Metabolomics Insights Into Antifungal Adaptationmentioning

confidence: 99%

What ‘Omics can tell us about antifungal adaptation

Ribeiro

Denes

Heaney

et al. 2021

FEMS Yeast Research

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Invasive candidiasis, the most frequent healthcare associated invasive fungal infection, is commonly caused by Candida albicans. However, in recent years other antifungal-resistant Candida species – namely C. glabrata and C. auris – have emerged as a serious matter of concern. Much of our understanding of the mechanisms regulating antifungal resistance and tolerance relies on studies utilising C. albicans, C. glabrata, and the model yeast Saccharomyces cerevisiae. ‘Omics studies have been used to describe alterations in metabolic, genomic and transcriptomic expression profiles upon antifungal treatment of fungal cells. The physiological changes identified by these approaches could significantly affect fungal fitness in the host and survival during antifungal challenge, as well as provide further understanding of clinical resistance. Thus, this review aims to comparatively address ‘omics data for C. albicans, C. glabrata, and S. cerevisiae published from 2000 to 2021 to identify what these technologies can tell us regarding cellular responses to antifungal therapy. We will also highlight possible effects on pathogen survival and identify future avenues for antifungal research.

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Proteomic analysis of cytosolic proteins associated with petite mutations in Candida glabrata

Cited by 7 publications

References 36 publications

Proteomic Analysis of Cellular and Membrane Proteins in Fluconazole-Resistant Candida glabrata

Proteomic Analysis of Cellular and Membrane Proteins in Fluconazole-Resistant Candida glabrata

Histatin 5 Resistance of Candida glabrata Can Be Reversed by Insertion of Candida albicans Polyamine Transporter-Encoding Genes DUR3 and DUR31

What ‘Omics can tell us about antifungal adaptation

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