ArticleGlycobiology2012
The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases.
Article in Glycobiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Mechanisms of Quality Control in GPI-Anchored Proteins: The Central Role of the Lipid Anchor.International journal of molecular sciences · 2026Review
- GLYCO-BUILD: an enzymatic pipeline for the synthesis of peptides carrying eukaryotic N-glycans.Nature communications · 2025Article
- Generation of a bloodstream form Trypanosoma brucei double glycosyltransferase null mutant competent in receptor-mediated endocytosis of transferrin.PLoS pathogens · 2024Article
- Molecular basis for glycan recognition and reaction priming of eukaryotic oligosaccharyltransferase.Nature communications · 2022Article
- Common and unique features of glycosylation and glycosyltransferases in African trypanosomes.The Biochemical journal · 2022Article
- Endoplasmic reticulum-associated degradation and disposal of misfolded GPI-anchored proteins in Trypanosoma brucei.Molecular biology of the cell · 2018Article
- Analysis of substrate specificity ofThe Journal of biological chemistry · 2017Article
- Single-subunit oligosaccharyltransferases ofThe Journal of biological chemistry · 2017Article
- Chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins.Glycobiology · 2017Article
- Characterization of the single-subunit oligosaccharyltransferase STT3A from Trypanosoma brucei using synthetic peptides and lipid-linked oligosaccharide analogs.Glycobiology · 2017Article
- RFT1 Protein Affects Glycosylphosphatidylinositol (GPI) Anchor Glycosylation.The Journal of biological chemistry · 2017Article
- SWATH-MS Glycoproteomics Reveals Consequences of Defects in the Glycosylation Machinery.Molecular & cellular proteomics : MCP · 2016Article
- A Gene of the β3-Glycosyltransferase Family Encodes N-Acetylglucosaminyltransferase II Function in Trypanosoma brucei.The Journal of biological chemistry · 2016Article
- N-glycoprotein macroheterogeneity: biological implications and proteomic characterization.Glycoconjugate journal · 2016Review
- Identification of a glycosylphosphatidylinositol anchor-modifying β1-3 galactosyltransferase in Trypanosoma brucei.Glycobiology · 2015Article
- Identification and functional characterization of a highly divergent N-acetylglucosaminyltransferase I (TbGnTI) in Trypanosoma brucei.The Journal of biological chemistry · 2014Article
- Article
- Intracellular trafficking and glycobiology of TbPDI2, a stage-specific protein disulfide isomerase in Trypanosoma brucei.Eukaryotic cell · 2013Article
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3 authors.
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Abstract
We recently presented a model for site-specific protein N-glycosylation in Trypanosoma brucei whereby the TbSTT3A oligosaccharyltransferase (OST) first selectively transfers biantennary Man(5)GlcNAc(2) from the lipid-linked oligosaccharide (LLO) donor Man(5)GlcNAc(2)-PP-Dol to N-glycosylation sequons in acidic to neutral peptide sequences and TbSTT3B selectively transfers triantennary Man(9)GlcNAc(2) to any remaining sequons. In this paper, we investigate the specificities of the two OSTs for their preferred LLO donors by glycotyping the variant surface glycoprotein (VSG) synthesized by bloodstream-form T. brucei TbALG12 null mutants. The TbALG12 gene encodes the α1-6-mannosyltransferase that converts Man(7)GlcNAc(2)-PP-Dol to Man(8)GlcNAc(2)-PP-Dol. The VSG synthesized by the TbALG12 null mutant in the presence and the absence of α-mannosidase inhibitors was characterized by electrospray mass spectrometry both intact and as pronase glycopetides. The results show that TbSTT3A is able to transfer Man(7)GlcNAc(2) as well as Man(5)GlcNAc(2) to its preferred acidic glycosylation site at Asn263 and that, in the absence of Man(9)GlcNAc(2)-PP-Dol, TbSTT3B transfers both Man(7)GlcNAc(2) and Man(5)GlcNAc(2) to the remaining site at Asn428, albeit with low efficiency. These data suggest that the preferences of TbSTT3A and TbSTT3B for their LLO donors are based on the c-branch of the Man(9)GlcNAc(2) oligosaccharide, such that the presence of the c-branch prevents recognition and/or transfer by TbSTT3A, whereas the presence of the c-branch enhances recognition and/or transfer by TbSTT3B.
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