Hydrophobic and hydrophilic cell surface (glyco)proteinic components of Candida albicans

Objective. Cell surface hydrophobicity (CSH) has been shown to influence ad hesion and virulence of the opportunistic fungal pathogen Candida albicans. The aim of this work was to identify the potential cell surface (glyco)pro teins supporting the relative CSH according to the morphological phase and culture conditions of Candida albicans. Material and methods. To characterize cell surface hydrophobic and hydrophi lic components, Candida albicans Zymolyase crude soluble extracts of germ t ubes and blastoconidia were fractionated by hydrophobic interaction chromat ography. Prior to extraction, Candida cells were biotinylated in order to l abel cell surface proteins and glycoproteins. Proteinic and glycosylated co mpounds of the fractionated extracts were then tested by SDS-PAGE and conca navalin A staining, and probed with streptavidin peroxidase conjugate. Results and conclusion. For both morphological phases, cell surface hydroph ilic fractions corresponded to highly glycosylated components of high molec ular masses (over 94-kDa) and to a 34-kDa glycoprotein, whereas hydrophobic material was mainly represented by proteins with molecular masses between 10- to 94-kDa. Cell surface glycosylated high molecular mass components wer e more slightly hydrophobic for blastoconidia grown at 22 degreesC than for yeasts grown at 37 degreesC. Chromatography allowed identification of two peculiar cell surface germ tube specific components: a glycosylated polydis persed material of 110- to 220-kDa, and a 30-kDa proteinic components. Thes e two hyphal phase specific components were characterized as being very hyd rophobic.