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A proteomic analysis of the salt, cadmium and peroxide stress responses in Candida albicans and the role of the Hog1 stress‐activated MAPK in regulating the stress‐induced proteome
Author(s) -
Yin Zhikang,
Stead David,
Walker Jan,
Selway Laura,
Smith Deborah A.,
Brown Alistair J. P.,
Quinn Janet
Publication year - 2009
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200800958
Subject(s) - candida albicans , proteome , corpus albicans , transcriptome , cadmium , chemistry , biology , proteomics , biochemistry , microbiology and biotechnology , gene expression , gene , organic chemistry
Stress responses are important for the virulence of the major fungal pathogen of humans, Candida albicans . In this study we employed a 2‐DE approach to examine the impact of exposure to peroxide (5 mM H 2 O 2 ), salt (300 mM NaCl) or cadmium stress (0.5 mM Cd 2+ ) upon the C. albicans proteome. Highly reproducible changes in the C. albicans proteome were observed in response to each stress condition. Significantly more proteins were up‐regulated in response to cadmium (77) than to the salt (35) or peroxide stresses (35). These proteomic changes displayed minimal overlap with those observed in the transcriptome under equivalent conditions and, importantly, revealed functional categories that respond to stress at the protein level but not the transcript level. Six proteins were up‐regulated by all three conditions: Adh1, Atp2, Cip1, Eft2, Ssa1 and Ssb1, which is consistent with the concept that a core stress response exists in C. albicans. This is the first time that a fungal core stress response has been defined at the proteomic level. We have also shown that the Hog1 stress‐activated mitogen‐activated protein kinase, which is activated in response to the stresses examined in this study, makes a major contribution to the C. albicans stress proteome.