Evidence for the formation of covalent bonds between macromolecules in the domain of the wall of Candida albicans mycelial cells.
An O-glycosylated mannoprotein, after its incorporation into the wall, showed an increase in its molecular weight, due at least to its association with N-glycosidic sugar chain(s). This was shown by rendering the material soluble after partial degradation of the wall structure. At present it is unknown whether this phenomenon is due to an additional transglycosylation process or whether the partial degradation of the wall solubilizes a supramolecular structure formed between the original O-glycosylated protein which becomes linked either directly or indirectly through a protein to the N-sugar chain(s).
Elorza
V
V
Department de Microbiologia, Facultat de Farmacia, Valencia, Spain.
Mormeneo
S
S
Garcia de la Cruz
F
F
Gimeno
C
C
Sentandreu
R
R
D000911:Antibodies, Monoclonal / Q000378:metabolism; D015153:Blotting, Western; D002176:Candida albicans / Q000648:ultrastructure*; D002473:Cell Wall / Q000378:metabolism* / Q000648:ultrastructure; D005656:Fungal Proteins / Q000378:metabolism* / Q000648:ultrastructure; D043326:Glucan 1,3-beta-Glucosidase; D006031:Glycosylation; D046911:Macromolecular Substances; D008562:Membrane Glycoproteins / Q000378:metabolism; D008970:Molecular Weight; D011499:Protein Processing, Post-Translational; D001617:beta-Glucosidase / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D005656:Fungal Proteins; D046911:Macromolecular Substances; D008562:Membrane Glycoproteins; C025363:mannoproteins; D001617:beta-Glucosidase; D043326:Glucan 1,3-beta-Glucosidase