Acceptor range of endo-β- N -acetylglucosaminidase mutant endo-CC N180H: from monosaccharide to antibody-Reference-Cited by-同舟云学术

Acceptor range of endo-β- N -acetylglucosaminidase mutant endo-CC N180H: from monosaccharide to antibody

Published:2018-05 Issue:5 Volume:5 Page:171521
ISSN:2054-5703
Container-title:Royal Society Open Science
language:en
Short-container-title:R. Soc. open sci.

Author:

Manabe Shino¹^ORCID,Yamaguchi Yoshiki²,Abe Junpei¹,Matsumoto Kana²,Ito Yukishige¹^ORCID

Affiliation:

1. Synthetic Cellular Chemistry Laboratory, RIKEN, Hirosawa, Wako, Saitama 351-0198, Japan

2. Structural Glycobiology Team, RIKEN, Hirosawa, Wako, Saitama 351-0198, Japan

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.

Funder

MEXT/JSPS KAKENHI

Japan Agency for Medical Research and Development

Publisher

The Royal Society

Subject

Multidisciplinary

Link

https://royalsocietypublishing.org/doi/pdf/10.1098/rsos.171521

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