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

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...

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Autores principales: Manabe, Shino, Yamaguchi, Yoshiki, Abe, Junpei, Matsumoto, Kana, Ito, Yukishige
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society Publishing 2018
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5990847/
https://www.ncbi.nlm.nih.gov/pubmed/29892355
http://dx.doi.org/10.1098/rsos.171521
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author Manabe, Shino
Yamaguchi, Yoshiki
Abe, Junpei
Matsumoto, Kana
Ito, Yukishige
author_facet Manabe, Shino
Yamaguchi, Yoshiki
Abe, Junpei
Matsumoto, Kana
Ito, Yukishige
author_sort Manabe, Shino
collection PubMed
description 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.
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spelling pubmed-59908472018-06-11 Acceptor range of endo-β-N-acetylglucosaminidase mutant endo-CC N180H: from monosaccharide to antibody Manabe, Shino Yamaguchi, Yoshiki Abe, Junpei Matsumoto, Kana Ito, Yukishige R Soc Open Sci Chemistry 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. The Royal Society Publishing 2018-05-16 /pmc/articles/PMC5990847/ /pubmed/29892355 http://dx.doi.org/10.1098/rsos.171521 Text en © 2018 The Authors. http://creativecommons.org/licenses/by/4.0/ Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.
spellingShingle Chemistry
Manabe, Shino
Yamaguchi, Yoshiki
Abe, Junpei
Matsumoto, Kana
Ito, Yukishige
Acceptor range of endo-β-N-acetylglucosaminidase mutant endo-CC N180H: from monosaccharide to antibody
title Acceptor range of endo-β-N-acetylglucosaminidase mutant endo-CC N180H: from monosaccharide to antibody
title_full Acceptor range of endo-β-N-acetylglucosaminidase mutant endo-CC N180H: from monosaccharide to antibody
title_fullStr Acceptor range of endo-β-N-acetylglucosaminidase mutant endo-CC N180H: from monosaccharide to antibody
title_full_unstemmed Acceptor range of endo-β-N-acetylglucosaminidase mutant endo-CC N180H: from monosaccharide to antibody
title_short Acceptor range of endo-β-N-acetylglucosaminidase mutant endo-CC N180H: from monosaccharide to antibody
title_sort acceptor range of endo-β-n-acetylglucosaminidase mutant endo-cc n180h: from monosaccharide to antibody
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5990847/
https://www.ncbi.nlm.nih.gov/pubmed/29892355
http://dx.doi.org/10.1098/rsos.171521
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