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Taxonomic group: fungi / Ascomycota (Phylum: Ascomycota)

Publication DOI: 10.1038/nrmicro1087
Journal NLM ID: 101190261
Publisher: London, UK: Nature Publishing Group
Correspondence: tillman.gerngross

dartmouth.edu
Institutions: GlycoFi Inc., 21 Lafayette Street, Lebanon,New Hampshire 03766, USA, Thayer School of Engineering, Department of Biological Sciences, and Department of Chemistry, Dartmouth College, Hanover,New Hampshire 03755, USA

Yeast and other fungal protein-expression hosts have been extensively used to produce industrial enzymes, and are often the expression system of choice when manufacturing costs are of primary concern. However, for the production of therapeutic glycoproteins intended for use in humans, yeast have been less useful owing to their inability to modify proteins with human glycosylation structures. Yeast N-glycosylation is of the high-mannose type, which confers a short half-life in vivo and thereby compromises the efficacy of most therapeutic glycoproteins. Several approaches to humanizing yeast N-glycosylation pathways have been attempted over the past decade with limited success. Recently however, advances in the glycoengineering of yeast and the expression of therapeutic glycoproteins with humanized N-glycosylation structures have shown significant promise-this review summarizes the most important developments in the field.

Saccharomyces-cerevisiae, asparagine-linked oligosaccharides, luminal ER proteins, Pichia-pastoris, Campylobacter-jejuni, rat-liver, glycoprotein-synthesis, endoplasmic-reticulum, ALG3 gene, Hansenula-polymorpha

Structure type: oligomer
Location inside paper: p.120, fig.1, Man9GlcNAc2, Golgi(yeast)
Aglycon: protein
Trivial name: glycoprotein
Compound class: glycoprotein
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_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_187201,IEDB_187238,IEDB_187239,IEDB_429156,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

Comments, role: review

Related record ID(s): 41281, 41283, 41284
NCBI Taxonomy refs (TaxIDs): 4932
Reference(s) to other database(s): GTC:G97455PT
Show glycosyltransferases

There is only one chemically distinct structure:

CC(=O)N[C@@H]1[C@@H](O)[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](CO)[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]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]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](CO)O[C@H]1O

SVG MW SMILES 3D mol Ionize