Covalent association of beta-1,3-glucan with beta-1,6-glucosylated mannoproteins in cell walls of Candida albicans.
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.
Kapteyn
J C
JC
Institute of Molecular Cell Biology, BioCentrum Amsterdam, University of Amsterdam, The Netherlands.
Montijn
R C
RC
Dijkgraaf
G J
GJ
Van den Ende
H
H
Klis
F M
FM
D000918:Antibody Specificity; D015153:Blotting, Western; D002176:Candida albicans / Q000737:chemistry* / Q000276:immunology; D002240:Carbohydrate Sequence; D002473:Cell Wall / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D000939:Epitopes; D004693:Glucan Endo-1,3-beta-D-Glucosidase / Q000378:metabolism; D005936:Glucans / Q000737:chemistry* / Q000276:immunology; D006031:Glycosylation; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000276:immunology; D008969:Molecular Sequence Data; D010755:Organophosphates; D047071:beta-Glucans
D000939:Epitopes; D005936:Glucans; D008562:Membrane Glycoproteins; D010755:Organophosphates; D047071:beta-Glucans; C025363:mannoproteins; C064197:beta-1,6-glucan; C033363:beta-1,3-glucan; D004693:Glucan Endo-1,3-beta-D-Glucosidase