N-glycosylation with synthetic undecaprenyl pyrophosphate-linked oligosaccharide to oligopeptides by PglB oligosaccharyltransferase from Campylobacter jejuni

Akihiro Ishiwata; Yuya Taguchi; Yong Joo Lee; Taisuke Watanabe; Daisuke Kohda; Yukishige Ito

doi:10.1002/cbic.201402658

N-glycosylation with synthetic undecaprenyl pyrophosphate-linked oligosaccharide to oligopeptides by PglB oligosaccharyltransferase from Campylobacter jejuni

Akihiro Ishiwata, Yuya Taguchi, Yong Joo Lee, Taisuke Watanabe, Daisuke Kohda, Yukishige Ito

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

The oligosaccharyltransferase PglB from Campylobacter jejuni catalyses the N-glycosylation reaction with undecaprenyl-pyrophosphate-linked Glc₁GalNAc₅Bac₁ (Und-PP-Glc₁GalNAc₅Bac₁). Experiments using chemically synthesized donors coupled to fluorescently tagged peptides confirmed that biosynthetic intermediate Und-PP-Bac₁ and Und-PP-GalNAc₂Bac₁ are transferred efficiently to the Asn residue in the consensus sequence (D/E-X'-N-X-T/S, X',X≠P). The products were analyzed in detail by tandem MS to confirm their chemical structures.

Original language	English
Pages (from-to)	731-737
Number of pages	7
Journal	ChemBioChem
Volume	16
Issue number	5
DOIs	https://doi.org/10.1002/cbic.201402658
Publication status	Published - Mar 23 2015

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Medicine
Molecular Biology
Organic Chemistry

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title = "N-glycosylation with synthetic undecaprenyl pyrophosphate-linked oligosaccharide to oligopeptides by PglB oligosaccharyltransferase from Campylobacter jejuni",

abstract = "The oligosaccharyltransferase PglB from Campylobacter jejuni catalyses the N-glycosylation reaction with undecaprenyl-pyrophosphate-linked Glc1GalNAc5Bac1 (Und-PP-Glc1GalNAc5Bac1). Experiments using chemically synthesized donors coupled to fluorescently tagged peptides confirmed that biosynthetic intermediate Und-PP-Bac1 and Und-PP-GalNAc2Bac1 are transferred efficiently to the Asn residue in the consensus sequence (D/E-X'-N-X-T/S, X',X≠P). The products were analyzed in detail by tandem MS to confirm their chemical structures.",

author = "Akihiro Ishiwata and Yuya Taguchi and Lee, {Yong Joo} and Taisuke Watanabe and Daisuke Kohda and Yukishige Ito",

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doi = "10.1002/cbic.201402658",

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T1 - N-glycosylation with synthetic undecaprenyl pyrophosphate-linked oligosaccharide to oligopeptides by PglB oligosaccharyltransferase from Campylobacter jejuni

AU - Ishiwata, Akihiro

AU - Taguchi, Yuya

AU - Lee, Yong Joo

AU - Watanabe, Taisuke

AU - Kohda, Daisuke

AU - Ito, Yukishige

PY - 2015/3/23

Y1 - 2015/3/23

N2 - The oligosaccharyltransferase PglB from Campylobacter jejuni catalyses the N-glycosylation reaction with undecaprenyl-pyrophosphate-linked Glc1GalNAc5Bac1 (Und-PP-Glc1GalNAc5Bac1). Experiments using chemically synthesized donors coupled to fluorescently tagged peptides confirmed that biosynthetic intermediate Und-PP-Bac1 and Und-PP-GalNAc2Bac1 are transferred efficiently to the Asn residue in the consensus sequence (D/E-X'-N-X-T/S, X',X≠P). The products were analyzed in detail by tandem MS to confirm their chemical structures.

AB - The oligosaccharyltransferase PglB from Campylobacter jejuni catalyses the N-glycosylation reaction with undecaprenyl-pyrophosphate-linked Glc1GalNAc5Bac1 (Und-PP-Glc1GalNAc5Bac1). Experiments using chemically synthesized donors coupled to fluorescently tagged peptides confirmed that biosynthetic intermediate Und-PP-Bac1 and Und-PP-GalNAc2Bac1 are transferred efficiently to the Asn residue in the consensus sequence (D/E-X'-N-X-T/S, X',X≠P). The products were analyzed in detail by tandem MS to confirm their chemical structures.

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N-glycosylation with synthetic undecaprenyl pyrophosphate-linked oligosaccharide to oligopeptides by PglB oligosaccharyltransferase from Campylobacter jejuni

Abstract

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