Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Microbiology 153 (2007), 2351-2362; DOI  10.1099/mic.0.2006/004028-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jezewski, S.
Right arrow Articles by Eck, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jezewski, S.
Right arrow Articles by Eck, R.
Agricola
Right arrow Articles by Jezewski, S.
Right arrow Articles by Eck, R.
Microbiology 153 (2007), 2351-2362; DOI  10.1099/mic.0.2006/004028-0
© 2007 Society for General Microbiology

Role of the Vps34p-interacting protein Ade5,7p in hyphal growth and virulence of Candida albicans

Susann Jezewski1,{dagger}, Monika von der Heide1, Sophia Poltermann1, Albert Härtl1, Waldemar Künkel2, Peter F. Zipfel1 and Raimund Eck2,{ddagger}

1 Leibniz Institute for Natural Products Research and Infection Biology/Hans Knöll Institute, Beutenbergstrasse 11, D-07745 Jena, Germany
2 University of Applied Sciences, Carl-Zeiss-Promenade 2, D-07745 Jena, Germany

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

The phosphatidylinositol (PtdIns) 3-kinase Vps34p of the human pathogenic yeast Candida albicans participates in virulence and in protein transport. In order to dissect these two functions, a search for proteins interacting with C. albicans Vps34p was performed using a yeast two-hybrid system. This study demonstrates the physical interaction between Vps34p and Ade5,7p, which is the bifunctional enzyme of the de novo purine nucleotide biosynthetic pathway. The interaction initially observed in a yeast two-hybrid system was confirmed in vitro with recombinant proteins. Given the complex formation between Ade5,7p and the virulence-regulating Vps34p, it was of interest to characterize the function of Ade5,7p in C. albicans. To this end, ade5,7 null mutants were generated. The resulting mutants were adenine deficient, and sensitive to the presence of metal ions. In addition, the ade5,7 null mutants were avirulent in a mouse model of systemic candidiasis, and showed reduced hyphal growth in an agar matrix under embedded conditions. In summary, Ade5,7p interacts with the multifunctional virulence regulator PtdIns 3-kinase Vps34p, and ade5,7 and vps34 null mutant strains show similar phenotypes regarding sensitivity to metal ions, hyphal growth and virulence.

Abbreviations: AD, activation domain of Gal4p; AIRS, aminoimidazole ribotide synthetase; BD, binding domain of the transcription factor Gal4p; EBP, oestrogen-binding protein; FCS, fetal calf serum; GAAC, general amino acid control; GARS, glycinamide ribotide synthetase; GST, glutathione S-transferase; P, plasma membrane; PtdIns, phosphatidylinositol; V, vacuolar; VHHFLU, antibody against fluorescein

{dagger}Present address: Friedrich Schiller University, Institute of Microbiology – Department of Microbial Phytopathology, Neugasse 25, D-07743 Jena, Germany.

{ddagger}Present address: SIRS-Lab GmbH, Winzerlaer Str. 2, D-07745 Jena, Germany.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2007 Society for General Microbiology.