Characterization Of Two Soluble (52 / 42 Kda) Glycoproteins Whose Pattern Is Up-Regulated During Yeast-To-Filament Growth Transition Of C. Albicans

AUTHORS

Mourad ER-RASFA 1 , *

1 Laboratoire de Pharmacologie, Faculte de Medecine et de Pharmacie, Universite Sidi Mo- hamed Ben Abdellah, Fez, 30000, Morocco

How to Cite: ER-RASFA M. Characterization Of Two Soluble (52 / 42 Kda) Glycoproteins Whose Pattern Is Up-Regulated During Yeast-To-Filament Growth Transition Of C. Albicans, Shiraz E-Med J. Online ahead of Print ; 8(3):110-119.

ARTICLE INFORMATION

Shiraz E-Medical Journal: 8 (3); 110-119
Published Online: July 1, 2007
Article Type: Research Article
Received: February 28, 2007
Accepted: April 2, 2007

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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.

© 2007, Author(s). This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International License (http://creativecommons.org/licenses/by-nc/4.0/) which permits copy and redistribute the material just in noncommercial usages, provided the original work is properly cited.

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