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 journalArticle

    3 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 languageEnglish
    Pages (from-to)731-737
    Number of pages7
    JournalChemBioChem
    Volume16
    Issue number5
    DOIs
    Publication statusPublished - Mar 23 2015

    All Science Journal Classification (ASJC) codes

    • Biochemistry
    • Molecular Medicine
    • Molecular Biology
    • Organic Chemistry

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