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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.
| Content Provider | Europe PMC |
|---|---|
| Author | Ashida, Hisashi Fujimoto, Taku Kurihara, Shin Nakamura, Masayuki Komeno, Masahiro Huang, Yibo Katayama, Takane Kinoshita, Takashi Takegawa, Kaoru |
| Abstract | 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. |
| Related Links | https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC8367633&blobtype=pdf |
| ISSN | 13447882 |
| Volume Number | 67 |
| PubMed Central reference number | PMC8367633 |
| Issue Number | 1 |
| PubMed reference number | 34429696 |
| Journal | Journal of Applied Glycoscience [J Appl Glycosci (1999)] |
| e-ISSN | 18807291 |
| DOI | 10.5458/jag.jag.jag-2019_0016 |
| Language | English |
| Publisher | The Japanese Society of Applied Glycoscience |
| Publisher Date | 2020-02-20 |
| Publisher Place | Tokyo, JAPAN |
| Access Restriction | Open |
| Rights License | This is an open-access paper distributed under the terms of the Creative Commons Attribution Non-Commercial (by-nc) License (CC-BY-NC4.0: https://creativecommons.org/licenses/by-nc/4.0/). 2020 by The Japanese Society of Applied Glycoscience |
| Subject Keyword | core fucose fucosidase GH29 gut bacteria probiotics |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry, Genetics and Molecular Biology |
