Localization and functional characterization of the pathogenesis-related proteins Rbe1p and Rbt4p in Candida albicans
Bantel, AnnickInstitute of Interfacial Process Engineering and Plasma Technology, University of Stuttgart, Germany
Darwiche, RabihDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, USA
Rupp, SteffenDepartment of Molecular Biotechnology, Fraunhofer IGB, Stuttgart, Germany
Schneiter, RogerDepartment of Biology, University of Fribourg, Switzerland
Sohn, KaiDepartment of Molecular Biotechnology, Fraunhofer IGB, Stuttgart, Germany
06.08.2018
Published in:
PLOS ONE. - 2018, vol. 13, no. 8, p. e0201932
English
Members of the Cysteine-rich secretory protein, Antigen 5 and Pathogenesis-related 1 (CAP) protein superfamily are important virulence factors in fungi but remain poorly characterized on molecular level. Here, we investigate the cellular localization and molecular function of Rbe1p and Rbt4p, two CAP family members from the human pathogen Candida albicans. We unexpectedly found that Rbe1p localizes to budding sites of yeast cells in a disulfide bond-dependent manner. Furthermore, we show that Rbe1p and Rbt4p bind free cholesterol in vitro and export cholesteryl acetate in vivo. These findings suggest a previously undescribed role for Rbe1p in cell wall- associated processes and a possible connection between the virulence attributes of fungal CAP proteins and sterol binding.