TY - JOUR
T1 - Essential role for vacuolar acidification in candida albicans virulence
AU - Patenaude, Cassandra
AU - Zhang, Yongqiang
AU - Cormack, Brendan
AU - Köhler, Julia
AU - Rao, Rajini
PY - 2013/9/6
Y1 - 2013/9/6
N2 - Background: V-ATPase is responsible for establishing electrochemical gradients through energy-dependent proton transport. Results: In Candida albicans, mutation of vph1 resulted in defective phenotypic switching and avirulence in a murine septicemia model. Conclusion: The vacuolar specific isoform Vph1 is essential for vacuolar acidification and virulence in Candida albicans. Significance: Acidification of the vacuole plays a unique role in fungal virulence and growth phenotype.
AB - Background: V-ATPase is responsible for establishing electrochemical gradients through energy-dependent proton transport. Results: In Candida albicans, mutation of vph1 resulted in defective phenotypic switching and avirulence in a murine septicemia model. Conclusion: The vacuolar specific isoform Vph1 is essential for vacuolar acidification and virulence in Candida albicans. Significance: Acidification of the vacuole plays a unique role in fungal virulence and growth phenotype.
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U2 - 10.1074/jbc.M113.494815
DO - 10.1074/jbc.M113.494815
M3 - Article
C2 - 23884420
AN - SCOPUS:84883715425
VL - 288
SP - 26256
EP - 26264
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 36
ER -