Open AccessThe β‐1,6‐glucan containing side‐chain of cell wall proteins of Saccharomyces cerevisiae is bound to the glycan core of the GPI moiety
Author(s) -
Der Vaart J. Marcel,
Te Biesebeke Rob,
Chapman John W.,
Klis Frans M.,
Verrips C. Theo
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08607.x
Subject(s) - glycan , moiety , saccharomyces cerevisiae , cell wall , biochemistry , glycosylation , epitope , cleavage (geology) , chemistry , side chain , protease , yeast , biology , glycoprotein , stereochemistry , enzyme , antibody , fracture (geology) , polymer , immunology , paleontology , organic chemistry
Cell wall proteins of Saccharomyces cerevisiae are anchored by means of a β‐1,6‐glucan‐containing side‐chain. It is not known whether this chain is linked to the protein part (e.g. through carbohydrate side‐chains) or to the glycosylphosphatidylinositol (GPI) moiety of cell wall proteins. An IgA protease recognition site was introduced in Cwp2p, a β‐1,6‐glucosylated cell wall protein, immediately N‐terminal from the omega amino acid (the attachment site of the GPI moiety). Proteolytic cleavage of this site revealed that the β‐1,6‐glucan epitope was not linked to the protein part. We conclude that neither N ‐ or O ‐glycosylation is involved in β‐glucosylation of cell wall proteins. This confirms that the glycan core of the GPI moiety is the probable β‐1,6‐glucan attachment site.