The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence.
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.
Poltermann
Sophia
S
Leibniz Institute for Natural Products Research and Infection Biology/Hans Knöll Institute, Department of Infection Biology, Beutenbergstrasse 11, D-07745 Jena, Germany.
Nguyen
Monika
M
Leibniz Institute for Natural Products Research and Infection Biology/Hans Knöll Institute, Department of Infection Biology, Beutenbergstrasse 11, D-07745 Jena, Germany.
Günther
Juliane
J
Leibniz Institute for Natural Products Research and Infection Biology/Hans Knöll Institute, Department of Infection Biology, Beutenbergstrasse 11, D-07745 Jena, Germany.
Wendland
Jürgen
J
Friedrich Schiller University, Department of Microbiology, D-07745 Jena, Germany.|Leibniz Institute for Natural Products Research and Infection Biology/Hans Knöll Institute, Department of Infection Biology, Beutenbergstrasse 11, D-07745 Jena, Germany.
Härtl
Albert
A
Leibniz Institute for Natural Products Research and Infection Biology/Hans Knöll Institute, Department of Infection Biology, Beutenbergstrasse 11, D-07745 Jena, Germany.
Künkel
Waldemar
W
University of Applied Sciences, Tatzendpromenade 1b, D-07745 Jena, Germany.
Zipfel
Peter F
PF
Leibniz Institute for Natural Products Research and Infection Biology/Hans Knöll Institute, Department of Infection Biology, Beutenbergstrasse 11, D-07745 Jena, Germany.
Eck
Raimund
R
Leibniz Institute for Natural Products Research and Infection Biology/Hans Knöll Institute, Department of Infection Biology, Beutenbergstrasse 11, D-07745 Jena, Germany.
D000818:Animals; D021461:Animals, Outbred Strains; D002176:Candida albicans / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development / Q000472:pathogenicity*; D002177:Candidiasis / Q000382:microbiology; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal; D006801:Humans; D006863:Hydrogen-Ion Concentration; D025301:Hyphae / Q000254:growth & development*; D008297:Male; D051379:Mice; D009154:Mutation; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism*; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014617:Vacuoles / Q000378:metabolism / Q000502:physiology*; D014774:Virulence
D005656:Fungal Proteins; D021122:Protein Subunits; D025262:Vacuolar Proton-Translocating ATPases