An Effective Bacterial Fucosidase for Glycoprotein Remodeling.
ACS Chem Biol
; 12(1): 63-72, 2017 01 20.
Article
em En
| MEDLINE
| ID: mdl-28103685
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bactérias
/
Imunoglobulina G
/
Glicoproteínas
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Fucose
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Alfa-L-Fucosidase
Limite:
Humans
Idioma:
En
Revista:
ACS Chem Biol
Ano de publicação:
2017
Tipo de documento:
Article
País de afiliação:
Taiwan