COVALENT ASSOCIATION OF BETA-1,3-GLUCAN WITH BETA-1,6-GLUCOSYLATED MANNOPROTEINS IN CELL-WALLS OF CANDIDA-ALBICANS

被引:89
作者
KAPTEYN, JC
MONTIJN, RC
DIJKGRAAF, GJP
VANDENENDE, H
KLIS, FM
机构
[1] Institute of Molecular Cell Biology, BioCentrum Amsterdam, University of Amsterdam, 1098 SM Amsterdam
关键词
D O I
10.1128/jb.177.13.3788-3792.1995
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:3788 / 3792
页数:5
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