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

Mourad ER-RASFA

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

Author(s):

Mourad ER-RASFA^1,*

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

Shiraz E-Medical Journal:Vol. 8, issue 3; 110-119

Published online:Jul 01, 2007

Article type:Research Article

Received:Feb 28, 2007

Accepted:Apr 02, 2007

How to Cite:Mourad ER-RASFACharacterization 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.8(3):110-119.

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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