Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: cell wall
NCBI PubMed ID: 7541400Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Institutions: Institute of Molecular Cell Biology, BioCentrum Amsterdam, University of Amsterdam, The Netherlands
Yeast and hyphal walls of Candida albicans were extracted with sodium dodecyl sulfate (SDS). Some of the extracted proteins reacted with a specific β-1,6-glucan antiserum but not with a β-1,3-glucan antiserum. They lost their β-1,6-glucan epitope after treatment with ice-cold aqueous hydrofluoric acid, suggesting that β-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 β-1,3-glucanase, several mannoproteins that were recognized by both the β-1,6-glucan antiserum and the β-1,3-glucan antiserum were released. Both epitopes were sensitive to aqueous hydrofluoric acid treatment, suggesting that β-1,3-glucan and β-1,6-glucan are linked to proteins by phosphodiester linkages. The possible role of β-glucans in the retention of cell wall proteins is discussed.
Structure type: homopolymer
Aglycon: P-linked mannoprotein
Contained glycoepitopes: IEDB_135614,IEDB_141806,IEDB_142488,IEDB_146664,IEDB_241101,IEDB_983931,SB_192
Methods: SDS-PAGE, Western blotting, enzymatic digestion, HF hydrolysis
Comments, role: epitope, fragment of a heteropolymer
Related record ID(s): 131843
NCBI Taxonomy refs (TaxIDs): 5476Reference(s) to other database(s): GTC:G26777BZ, CCSD:
43182, CBank-STR:1032
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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