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Microbiology 151 (2005), 1645-1655; DOI  10.1099/mic.0.27505-0
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Microbiology 151 (2005), 1645-1655; DOI  10.1099/mic.0.27505-0
© 2005 Society for General Microbiology

The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence

Sophia Poltermann1, Monika Nguyen1, Juliane Günther1, Jürgen Wendland1,3, Albert Härtl1, Waldemar Künkel2, Peter F. Zipfel1 and Raimund Eck1

1 Leibniz Institute for Natural Products Research and Infection Biology/Hans Knöll Institute, Department of Infection Biology, Beutenbergstrasse 11, D-07745 Jena, Germany
2 University of Applied Sciences, Tatzendpromenade 1b, D-07745 Jena, Germany
3 Friedrich Schiller University, Department of Microbiology, D-07745 Jena, Germany

Correspondence
Raimund Eck
raimund.eck{at}hki-jena.de

The vacuolar H+-ATPase (V-ATPase) component Vma7p of the human-pathogenic yeast Candida albicans regulates hyphal growth induced by serum and Spider medium and is essential for virulence. In order to characterize the functions of the putative V-ATPase subunit Vma7p of C. albicans, null mutants were generated. The resulting mutants showed reduced vacuole acidification, which correlated with defective growth at alkaline pH. In addition, defects in degradation of intravacuolar putative endosomal structures were observed. vma7 null mutants were sensitive towards the presence of metal ions. It is concluded that the sequestration of toxic ions in the vacuole via a H+ gradient generated by the V-ATPase is affected. The vma7 null mutant strains were avirulent in a mouse model of systemic candidiasis. In addition, C. albicans vma7 null mutants and the null mutant strain of the Vma7p-interacting phosphatidylinositol 3-kinase Vps34p showed similar phenotypes. In summary, the V-ATPase subunit Vma7p is involved in vacuolar ion transport and this transport is required for hyphal growth and virulence of C. albicans.

Abbreviations: PI, phosphatidylinositol; V-ATPase, vacuolar H+-ATPase




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