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JAC Advance Access published online on May 30, 2006
Journal of Antimicrobial Chemotherapy, doi:10.1093/jac/dkl221
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© The Author 2006. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org
Received May 3, 2006
Accepted May 5, 2006

Brief report

Proteomic analysis of experimentally induced azole resistance in Candida glabrata

P. David Rogers 1 *, John-Paul Vermitsky 2, Thomas D. Edlind 2, and George M. Hilliard 3

1 Department of Pharmacy, College of Pharmacy, University of Tennessee Health Science Center, Memphis, TN 38163, USA; Department of Pharmaceutical Sciences, College of Pharmacy, University of Tennessee Health Science Center, Memphis, TN 38163, USA; Department of Pediatrics, College of Medicine, University of Tennessee Health Science Center, Memphis, TN 38163, USA; Children's Foundation Research Center at Le Bonheur Children's Medical Center, Memphis, TN 38103, USA
2 Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129, USA
3 Department of Molecular Sciences, College of Medicine, University of Tennessee Health Science Center, Memphis, TN 38163, USA

* To whom correspondence should be addressed.
P. David Rogers, E-mail: drogers{at}utmem.edu


  Abstract

Objectives: The aim of the present study was to identify changes in the proteome of a laboratory-derived azole-resistant strain of Candida glabrata compared with its susceptible parent strain in an effort to identify proteins that are differentially expressed in association with azole resistance.

Methods: Soluble and membrane protein fractions were isolated from mutant strain F15 (fluconazole MIC > 128 mg/L) and parent strain 66032 (fluconazole MIC = 16 mg/L) grown to mid-log phase. Soluble proteins were resolved by both two-dimensional (2D) and one-dimensional (1D) polyacrylamide gel electrophoresis (GE) whereas membrane proteins were resolved by 1D GE. Spots or bands representing differentially expressed proteins were identified by matrix-assisted desorption ionization-time of flight mass spectroscopy (MALDI-TOF MS) and peptide mass fingerprinting.

Results: A total of 22 proteins were found to be more abundantly represented, and 3 proteins were found to be less abundantly represented, in strain F15 compared with strain 66032. These included up-regulation of the ATP-binding cassette transporter Cdr1p, the ergosterol biosynthesis enzyme Erg11p, proteins involved in glycolysis and glycerol metabolism, and proteins involved in the response to oxidative stress and cadmium exposure.

Conclusions: In addition to transcriptional regulation of Cdr1p, this study identified the differential expression of several proteins that may contribute to azole resistance and suggests the possibility for a post-transcriptional mechanism for increased expression of Erg11p.

Keywords: lanosterol demethylase; efflux pumps; antifungals.
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