Covalent association of beta-1,3-glucan with beta-1,6-glucosylated mannoproteins in cell walls of Candida albicans.

Abstract:

:Yeast and hyphal walls of Candida albicans were extracted with sodium dodecyl sulfate (SDS). Some of the extracted proteins reacted with a specific beta-1,6-glucan antiserum but not with a beta-1,3-glucan antiserum. They lost their beta-1,6-glucan epitope after treatment with ice-cold aqueous hydrofluoric acid, suggesting that beta-1,6-glucan was linked to the protein through a phosphodiester bridge. When yeast and hyphal walls extracted with SDS were subsequently extracted with a pure beta-1,3-glucanase, several mannoproteins that were recognized by both the beta-1,6-glucan antiserum and the beta-1,3-glucan antiserum were released. Both epitopes were sensitive to aqueous hydrofluoric acid treatment, suggesting that beta-1,3-glucan and beta-1,6-glucan are linked to proteins by phosphodiester linkages. The possible role of beta-glucans in the retention of cell wall proteins is discussed.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Kapteyn JC,Montijn RC,Dijkgraaf GJ,Van den Ende H,Klis FM

doi

10.1128/jb.177.13.3788-3792.1995

subject

Has Abstract

pub_date

1995-07-01 00:00:00

pages

3788-92

issue

13

eissn

0021-9193

issn

1098-5530

journal_volume

177

pub_type

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