Acceptor range of endo-β-N-acetylglucosaminidase mutant endo-CC N180H: from monosaccharide to antibody. Issue 5 (16th May 2018)

• Record Type: Journal Article
• Authors: Manabe, Shino; Yamaguchi, Yoshiki; Abe, Junpei; Matsumoto, Kana; Ito, Yukishige
• Is Part Of: Royal Society open science. Volume 5:Issue 5(2018)
• Publication Date: 2018-05-16
• Subjects: endo-β-N-acetylglucosaminidase mutant -- endo-CC N180H -- glycan transfer -- antibody -- sialylglycopeptide; Science -- Periodicals; 500
• DOI: 10.1098/rsos.171521
• Languages: English
• ISSNs: 2054-5703

Abstract

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.