Proteomic analysis of azole resistance in Candida albicans clinical isolates.
Changes in protein expression within a matched set of Candida albicans isolates representing the acquisition of azole resistance were examined by two-dimensional polyacrylamide gel electrophoresis and peptide mass fingerprinting. Proteins differentially expressed in association with azole resistance included Grp2p, Ifd1p, Ifd4p, Ifd5p, and Erg10p, a protein involved in the ergosterol biosynthesis pathway.
Hooshdaran
Massoumeh Z
MZ
Department of Pharmacy, College of Pharmacy, University of Tennessee Health Science Center, Memphis, TN 38163, USA.
Barker
Katherine S
KS
Hilliard
George M
GM
Kusch
Harald
H
Morschhäuser
Joachim
J
Rogers
P David
PD
D000603:Amino Acids, Sulfur / Q000096:biosynthesis / Q000378:metabolism; D000935:Antifungal Agents / Q000494:pharmacology*; D001393:Azoles / Q000494:pharmacology*; D002176:Candida albicans / Q000187:drug effects* / Q000235:genetics*; D002177:Candidiasis / Q000382:microbiology*; D025141:Drug Resistance, Fungal; D004591:Electrophoresis, Polyacrylamide Gel; D005800:Genes, Fungal / Q000235:genetics; D006801:Humans; D010449:Peptide Mapping; D040901:Proteomics; D015854:Up-Regulation / Q000187:drug effects
D000603:Amino Acids, Sulfur; D000935:Antifungal Agents; D001393:Azoles