1,6-α-L-Fucosidases from <i>Bifidobacterium</i> <i>longum</i> subsp. <i>infantis</i> ATCC 15697 Involved in the Degradation of Core-fucosylated <i>N</i>-Glycan
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- Ashida Hisashi
- Faculty of Biology-Oriented Science and Technology, Kindai University
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- Fujimoto Taku
- Graduate School of Biostudies, Kyoto University
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- Kurihara Shin
- Faculty of Biology-Oriented Science and Technology, Kindai University
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- Nakamura Masayuki
- Faculty of Biology-Oriented Science and Technology, Kindai University
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- Komeno Masahiro
- Faculty of Biology-Oriented Science and Technology, Kindai University
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- Huang Yibo
- Faculty of Agriculture, Kyushu University
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- Katayama Takane
- Graduate School of Biostudies, Kyoto University
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- Kinoshita Takashi
- Fushimi Pharmaceutical Co., Ltd.
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- Takegawa Kaoru
- Faculty of Agriculture, Kyushu University
Bibliographic Information
- Other Title
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- 1,6-α-L-Fucosidases from Bifidobacterium longum subsp. infantis ATCC 15697 Involved in the Degradation of Core-fucosylated N-Glycan
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Abstract
<p>Bifidobacterium longum subsp. infantis ATCC 15697 possesses five α-L-fucosidases, which have been previously characterized toward fucosylated human milk oligosaccharides containing α1,2/3/4-linked fucose [Sela et al.: Appl. Environ. Microbiol., 78, 795-803 (2012)]. In this study, two glycoside hydrolase family 29 α-L-fucosidases out of five (Blon_0426 and Blon_0248) were found to be 1,6-α-L-fucosidases acting on core α1,6-fucose on the N-glycan of glycoproteins. These enzymes readily hydrolyzed p-nitrophenyl-α-L-fucoside and Fucα1-6GlcNAc, but hardly hydrolyzed Fucα1-6(GlcNAcβ1-4)GlcNAc, suggesting that they de-fucosylate Fucα1-6GlcNAcβ1-Asn-peptides/proteins generated by the action of endo-β-N-acetylglucosaminidase. We demonstrated that Blon_0426 can de-fucosylate Fucα1-6GlcNAc-IgG prepared from Rituximab using Endo-CoM from Cordyceps militaris. To generate homogenous non-fucosylated N-glycan-containing IgG with high antibody-dependent cellular cytotoxicity (ADCC) activity, the resulting GlcNAc-IgG has a potential to be a good acceptor substrate for the glycosynthase mutant of Endo-M from Mucor hiemalis. Collectively, our results strongly suggest that Blon_0426 and Blon_0248 are useful for glycoprotein glycan remodeling.</p>
Journal
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 67 (1), 23-29, 2020-02-20
The Japanese Society of Applied Glycoscience
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Details 詳細情報について
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- CRID
- 1390283659852924672
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- NII Article ID
- 130007800497
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- NII Book ID
- AA11809133
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- ISSN
- 18807291
- 13447882
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- NDL BIB ID
- 030296280
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed