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Differential surface localization and temperature-dependent expression of the Candida albicans CSH1 protein

¹ Department of Pathology, University of Virginia Health System, PO Box 800904, Charlottesville, VA 22908-0904, USA
² Department of Microbiology, University of Virginia Health System, PO Box 800904, Charlottesville, VA 22908-0904, USA

Correspondence
Kevin C. Hazen
khazen{at}virginia.edu

Cell-surface hydrophobicity (CSH) in Candida albicans contributes to virulence and can be conveniently regulated in planktonic cultures by altering growth temperature. The CSH1 gene is the first candidate gene that has been demonstrated to play a role in affecting the CSH phenotype. However, the primary amino acid sequence of the CSH1 gene product suggests that the protein should be restricted to the cytoplasm. A majority of the protein appears to demonstrate that localization. Cell-surface biotinylation and limited glucanase digestion were used to determine and estimate the relative amount of Csh1p in the extracellular compartment in comparison to the cytoplasmic pool. Additionally, Western and Northern blotting were used to assess expression of the CSH1 gene under different growth conditions. Compared with cells grown at 23 °C, the total cellular levels of Csh1p are significantly greater at elevated growth temperatures. Detection of Csh1p on the cell surface correlates with the level of overall protein expression. The temperature-dependent regulation and surface presentation of Csh1p suggests a mechanism for regulating the CSH phenotype.

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