Defective Hyphal Induction of a Candida albicans Phosphatidylinositol 3-Phosphate 5-Kinase Null Mutant on Solid Media Does Not Lead to Decreased Virulence

Author:

Augsten Martin1,Hübner Claudia1,Nguyen Monika1,Künkel Waldemar12,Härtl Albert3,Eck Raimund1

Affiliation:

1. Department of Infection Biology

2. University of Applied Sciences, D-07745 Jena, Germany

3. Department of Drug Testing, Hans Knöll Institute for Natural Products Research

Abstract

ABSTRACT A phosphatidylinositol 3-phosphate [PI(3)P] 5-kinase gene ( CaFAB1 ) of the most important human pathogenic yeast, Candida albicans , was cloned and sequenced. An open reading frame was detected which encodes a 2,369-amino-acid protein with a calculated molecular mass of 268 kDa and a relative isoelectric point of 6.76. This protein exhibits 38% overall amino acid sequence identity with Saccharomyces cerevisiae Fab1p. We localized the CaFAB1 gene on chromosome R. To determine the influence of the PI(3)P 5-kinase CaFab1p on processes involved in C. albicans morphogenesis and pathogenicity, we sequentially disrupted both copies of the gene. Homozygous deletion of C. albicans CaFAB1 resulted in a mutant strain which exhibited defects in morphogenesis. A Cafab1 null mutant had enlarged vacuoles, an acidification defect, and increased generation times and was unable to form hyphae on different solid media. The sensitivities to hyperosmotic and high-temperature stresses, adherence, and virulence compared to those of wild-type strain SC5314 were not affected.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

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