Abstract
In this study, we sought to investigate the pattern of cellular glycoproteins during yeast-to-filament growth transition in Candida albicans, in vitro. By mean of glycoprotein extraction with Concanavalin A-Sepharose, and Western Blot analysis with peroxidase-labeled lectins (concanavalin A, wheat germ agglutinin), we have characterized two glycoproteins (52 kDa and 42 kDa) whose pattern is increased in the filamentous form of C.albicans. Analysis of subcellular fractions of C.albicans showed that the 52/42 kDa glycoproteins are located in the soluble fraction. in vitro treatment of concanavalin A-Sepharose extracted 52/42 kDa glycoproteins with the peptide N-linked glycosidase F showed that the 52 kDa protein is highly N-glycosylated and mannose 0-glycosylated, whereas the 42 kDa is N-glycosylated. Regulation of synthesis and / or glycosylation of the 52/42 kDa glycoproteins could be associated with yeast-to-filament growth transition of C.albicans.
Keywords
C.albicans filamentous growth protein glycosylation concanavalin A wheat germ agglutinin.
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© 2007, Author(s). This open-access article is available under the Creative Commons Attribution 4.0 (CC BY 4.0) International License (https://creativecommons.org/licenses/by/4.0/), which allows for unrestricted use, distribution, and reproduction in any medium, provided that the original work is properly cited.