The use of trypsin to solubilize wall proteins from Candida albicans led to the identification of chitinase 2 as an enzyme covalently linked to the yeast wall structure.
The use of trypsin to break proteins covalently linked to the yeast walls of Candida albicans released approx. 50% of the proteins, but also glucose and N-acetylglucosamine. Analysis by affinity chromatography indicated that glucose and/or N-acetylglucosamine formed part of the same supramolecular complexes with mannoproteins. These complexes would represent a new type of cell wall structuration in which beta-1,6 glucan and chitin are linked to proteins. An internal peptide from a 50-kDa protein released by trypsin was sequenced, showing 100% identity with chitinase 2 protein and 92% with chitinase 3. The electrophoretic mobility of the chitinase 2 protein was changed by treatment with EndoH or beta-elimination, indicating that the enzyme was both N- and O-mannosylated.
Iranzo
Maria
M
Sección de Microbiología, Facultad de Farmacia, Universidad de Valencia, Burajassot, Spain.
Aguado
Carmen
C
Pallotti
Claudia
C
Cañizares
José V
JV
Mormeneo
Salvador
S
D000595:Amino Acid Sequence; D001483:Base Sequence; D002176:Candida albicans / Q000201:enzymology*; D002473:Cell Wall / Q000737:chemistry / Q000201:enzymology; D002688:Chitinases / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D012995:Solubility; D014357:Trypsin / Q000378:metabolism
D005656:Fungal Proteins; D002688:Chitinases; D014357:Trypsin