Acceptor range of endo-β-n-acetylglucosaminidase mutant endo-CC N180H: From monosaccharide to antibody

Shino Manabe, Yoshiki Yamaguchi, Junpei Abe, Kana Matsumoto, Yukishige Ito

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The endo-β-N-acetylglucosaminidase mutant endo-CC N180H transfers glycan from sialylglycopeptide (SGP) to various acceptors. The scope and limitations of low-molecular-weight acceptors were investigated. Several homogeneous glycan-containing compounds, especially those with potentially useful labels or functional moieties, and possible reagents in glycoscience were synthesized. The 1,3-diol structure is important in acceptor molecules in glycan transfer reactions mediated by endo-CC N180H as well as by endo-M-N175Q. Glycan remodelling of antibodies was explored using core-fucose-deficient anti-CCR4 antibody with SGP and endo-CC N180H. Homogeneity of the glycan in the antibody was confirmed by mass spectrometry without glycan cleavage.

Original languageEnglish
Article number171521
JournalRoyal Society Open Science
Volume5
Issue number5
DOIs
Publication statusPublished - 2018 May 16
Externally publishedYes

Keywords

  • Antibody
  • Endo-CC N180H
  • Endo-β-N-acetylglucosaminidase mutant
  • Glycan transfer
  • Sialylglycopeptide

ASJC Scopus subject areas

  • General

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