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Taxonomic group: fungi / Ascomycota (Phylum: Ascomycota)

Publication DOI: 10.1093/glycob/cwh080
Journal NLM ID: 9104124
Publisher: IRL Press at Oxford University Press
Correspondence: marc.claeyssens

ugent.be
Institutions: Department of Biochemistry, Physiology and Microbiology, Ghent University, K.L. Ledeganckstraat 35, B-9000 Ghent, Belgium, Department of Molecular Biomedical Research, Ghent University, Flanders Interuniversity Institute for Biotechnology (VIB), Technologiepark 927, B-9052 Ghent (Zwijnaarde), Belgium

The glycosylation of Cel7A (CBH I) from Trichoderma reesei varies considerably when the fungus is grown under different conditions. As shown by ESI-MS and PAG-IEF analyses of both intact protein and the isolated catalytic core module, the microheterogeneity originates mainly from the variable ratio of single N-acetylglucosamine over high-mannose structures on the three N-glycosylation sites and from the presence or absence of phosphate residues. Fully N- and O-glycosylated Cel7A can only be isolated from minimal medium and probably reflects the initial complexity of the protein on leaving the glycosynthetic pathway. Extracellular activities are responsible for postsecretorial modifications in other cultivation conditions: alpha-(1-->2)-mannosidase, alpha-(1-->3)-glucosidase and an Endo H type activity participate in N-deglycosylation (core), whereas a phosphatase and a mannosidase are probably responsible for hydrolysis of O-glycans (linker). The effects are most prominent in corn steep liquor-enriched media, where the pH is closer to the pH optimum (5-6) of these extracellular hydrolases. In minimal medium, the low pH and the presence of proteases could explain for the absence of such activities. On the other hand, phosphodiester linkages in the catalytic module are only observed under specific conditions. The extracellular trigger is still unknown, but mannophosphorylation may be regulated intracellularly by alpha-(1-->2)-mannosidases and phosphomannosyl transferases competing for the same intermediate in the glycosynthetic pathway.

endoglycosidase, Trichoderma reesei, Cel7A, N- and O-glycosylation, postsecretorial modifications

Structure type: oligomer
Location inside paper: p.720, fig.11, A
Trivial name: core oligosaccharide
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_144996,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_187201,IEDB_429156,IEDB_474450,IEDB_540671,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85

Methods: SDS-PAGE, enzymatic hydrolysis, ESI-MS, biochemical methods, HPAEC-PAD, enzymatic analysis, DSA-FACE, IEF-PAGE
Comments, role: Core N-glycan structure of mannoproteins from S. cerevisiae MNN1.

Related record ID(s): 41303
NCBI Taxonomy refs (TaxIDs): 4932
Reference(s) to other database(s): GTC:G84902PL
Show glycosyltransferases

There is only one chemically distinct structure:

CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO)[C@@H](O[C@@H]3O[C@H](CO[C@H]4O[C@H](CO[C@H]5O[C@H](COP(=O)(O)O[C@H]6O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]6O)[C@@H](O)[C@H](O)[C@@H]5O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H](O)[C@H](O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H]4O)[C@@H](O)[C@H](O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](COP(=O)(O)O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O)[C@@H]3O)[C@H](O)[C@H]2NC(C)=O)[C@@H]1O

SVG MW SMILES 3D mol Ionize

endoglycosidase, Trichoderma reesei, Cel7A, N- and O-glycosylation, postsecretorial modifications

Structure type: oligomer
Location inside paper: p.720, fig.11, B
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141830,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144996,IEDB_144998,IEDB_146664,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_187201,IEDB_429156,IEDB_474450,IEDB_540671,IEDB_548907,IEDB_857734,IEDB_983930,IEDB_983931,SB_136,SB_192,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85

Methods: SDS-PAGE, enzymatic hydrolysis, ESI-MS, biochemical methods, HPAEC-PAD, enzymatic analysis, DSA-FACE, IEF-PAGE
Comments, role: Phosphorylated N-glycans on Cel7A of T. reesei RutC-30.

Related record ID(s): 41302
NCBI Taxonomy refs (TaxIDs): 1344414
Reference(s) to other database(s): GTC:G21124OF
Show glycosyltransferases

There is only one chemically distinct structure:

CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO)[C@@H](O[C@@H]3O[C@H](CO[C@H]4O[C@H](CO[C@H]5O[C@H](COP(=O)(O)O[C@H]6O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]6O)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H](O)[C@H](O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H]4O)[C@@H](O)[C@H](O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@H]5O)[C@@H]4O)[C@@H]3O)[C@H](O)[C@H]2NC(C)=O)[C@@H]1O

SVG MW SMILES 3D mol Ionize