Overview of N- and O-linked oligosaccharide structures found in various yeast species
Abstract
Yeast and most higher eukaryotes utilize an evolutionarily conserved N-linked oligosaccharide biosynthetic pathway that involves the formation of a Glc3Man9GlcNAc2-PP-dolichol lipid-linked precursor, the glycan portion of which is co-translationally transferred in the endoplasmic reticulum (ER) to suitable Asn residues on nascent polypeptides. Subsequently, ER processing glycohydrolases remove the three glucoses and, with the exception of Schizosaccharomyces pombe, a single, specific mannose residue. Processing sugar transferases in the Golgi lead to the formation of core-sized structures (Hex<15GlcNac2) as well as cores with an extended poly-alpha1,6-Man 'backbone' that is derivatized with various carbohydrate side chains in a species-specific manner (Hex50-200GlnNAc2). In some cases these are short alpha1,2-linked Man chains with (Saccharomyces cerevisiae) or without (Pichia pastoris) alpha1,3-Man caps, while in other yeast (S. pombe), the side chains are alpha1,2-linked Gal, some of which are capped with beta-1,3-linked pyruvylated Gal residues. Charged groups are also found in S. cerevisiae and P. pastoris N-glycans in the form of mannose phosphate diesters. Some pathogenic yeast (Candida albicans) add poly-beta1,2-Man extension through a phosphate diester to their N-glycans, which appears involved in virulence. O-Linked glycan synthesis in yeast, unlike in animal cells where it is initiated in the Golgi using nucleotide sugars, begins in the ER by addition of a single ma…
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Yeast cells produce glycoproteins with high-mannose glycan structures, which may be immunogenic and less potent in humans.
“However, these cells produce glycoproteins with high-mannose glycans structures, which may be immunogenic and less potent in humans (Dean, 1999;Gemmill and Trimble, 1999;Gerngross, 2004;Dumont et al., 2015).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Gemmill and Trimble, 1999
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- Authors
- Gemmill, T. R., & Trimble, R. B.
- Affiliations
- New York State Department of Health (US)
- Corresponding author
- Trimble, Robert B.
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 1999-01
- Volume
- 1426
- Issue
- 2
- Pages
- 227-237
- ISSN
- 0304-4165 (ISSN-L)
- OpenAlex
- W2007432405
- Cited by
- 439
- References
- 86
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 5 · 2023: 8 · 2022: 13 · 2021: 18 · 2020: 17 · 2019: 9 · 2018: 18 · 2017: 10 · 2016: 17 · 2015: 14 · 2014: 21 · 2013: 15 · 2012: 16
- FWCI
- 5.36
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - General Subjects (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01gm023900-26)
- U.S. Public Health Service
- National Institute of General Medical Sciences (GM23900)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Keywords
- N-glycosylation, O-glycosylation, Candida albicans, Pichia pastoris, Schizosaccharomyces pombe, Saccharomyces cerevisiae, glycoside hydrolases
- MeSH terms
- Candida albicans, Carbohydrate Sequence, Glycoproteins, Glycosylation, Molecular Sequence Data, Oligosaccharides, Pichia, Saccharomyces cerevisiae, Schizosaccharomyces, Yeasts
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