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The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases

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The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases. / Izquierdo, Luis; Mehlert, Angela; Ferguson, Michael A. J.

In: Glycobiology, Vol. 22, No. 5, 05.2012, p. 696-703.

Research output: Contribution to journalArticle

Harvard

Izquierdo, L, Mehlert, A & Ferguson, MAJ 2012, 'The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases' Glycobiology, vol 22, no. 5, pp. 696-703., 10.1093/glycob/cws003

APA

Izquierdo, L., Mehlert, A., & Ferguson, M. A. J. (2012). The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases. Glycobiology, 22(5), 696-703. 10.1093/glycob/cws003

Vancouver

Izquierdo L, Mehlert A, Ferguson MAJ. The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases. Glycobiology. 2012 May;22(5):696-703. Available from: 10.1093/glycob/cws003

Author

Izquierdo, Luis; Mehlert, Angela; Ferguson, Michael A. J. / The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases.

In: Glycobiology, Vol. 22, No. 5, 05.2012, p. 696-703.

Research output: Contribution to journalArticle

Bibtex - Download

@article{cdfdcb58bc4d493ba46f059fc9e5dbe0,
title = "The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases",
author = "Luis Izquierdo and Angela Mehlert and Ferguson, {Michael A. J.}",
year = "2012",
doi = "10.1093/glycob/cws003",
volume = "22",
number = "5",
pages = "696--703",
journal = "Glycobiology",
issn = "0959-6658",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases

A1 - Izquierdo,Luis

A1 - Mehlert,Angela

A1 - Ferguson,Michael A. J.

AU - Izquierdo,Luis

AU - Mehlert,Angela

AU - Ferguson,Michael A. J.

PY - 2012/5

Y1 - 2012/5

N2 - <p>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 alpha 1-6-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 alpha-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.</p>

AB - <p>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 alpha 1-6-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 alpha-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.</p>

U2 - 10.1093/glycob/cws003

DO - 10.1093/glycob/cws003

M1 - Article

JO - Glycobiology

JF - Glycobiology

SN - 0959-6658

IS - 5

VL - 22

SP - 696

EP - 703

ER -

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