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ACS Chem Biol. 2017 Jan 20;12(1):63-72. doi: 10.1021/acschembio.6b00821. Epub 2016 Nov 18.

An Effective Bacterial Fucosidase for Glycoprotein Remodeling.

Author information

1
Genomics Research Center, Academia Sinica , No. 128, Section 2, Academia Road, Taipei 115, Taiwan.
2
Institute of Biotechnology, National Taiwan University , Taipei 106, Taiwan.
3
Department of Chemistry, The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla, California 92037, United States.
4
Department of Chemistry, University of Michigan , Ann Arbor, Michigan 48109, United States.
5
CHO Pharma Inc. , Taipei 11503, Taiwan.

Abstract

Fucose is an important component of many oligo- and polysaccharide structures as well as glycoproteins and glycolipids, which are often associated with a variety of physiological processes ranging from fertilization, embryogenesis, signal transduction, and disease progression, such as rheumatoid arthritis, inflammation, and cancer. The enzyme α-l-fucosidase is involved in the cleavage of the fucosidic bond in glycans and glycoconjugates, particularly the Fuc-α-1,2-Gal, Fuc-α-1,3/4-GlcNAc, and Fuc-α-1,6-GlcNAc linkages. Here, we report a highly efficient fucosidase, designated as BfFucH identified from a library of bacterial glycosidases expressed in E. coli from the CAZy database, which is capable of hydrolyzing the aforementioned fucosidic linkages, especially the α-1,6-linkage from the N-linked Fuc-α-1,6-GlcNAc residue on glycoproteins. Using BfFucH coupled with endoglycosidases and the emerging glycosynthases allows glycoengineering of IgG antibodies to provide homogeneous glycoforms with well-defined glycan structures and optimal effector functions.

PMID:
28103685
DOI:
10.1021/acschembio.6b00821
[Indexed for MEDLINE]

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