We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Identification and characterization of a sulfoglycosidase from Bifidobacterium bifidum implicated in mucin glycan utilization.
- Authors
Katoh, Toshihiko; Maeshibu, Takako; Kikkawa, Kei-ichi; Gotoh, Aina; Tomabechi, Yusuke; Nakamura, Motoharu; Liao, Wei-Hsiang; Yamaguchi, Masanori; Ashida, Hisashi; Yamamoto, Kenji; Katayama, Takane
- Abstract
Human gut symbiont bifidobacteria possess carbohydrate-degrading enzymes that act on theO-linked glycans of intestinal mucins to utilize those carbohydrates as carbon sources. However, our knowledge about mucin typeO-glycan degradation by bifidobacteria remains fragmentary, especially regarding how they decompose sulfated glycans, which are abundantly found in mucin sugar-chains. Here, we examined the abilities of severalBifidobacteriumstrains to degrade a sulfated glycan substrate and identified a 6-sulfo-β-d-N-acetylglucosaminidase, also termed sulfoglycosidase, encoded bybbhIIfromBifidobacterium bifidumJCM 7004. A recombinant BbhII protein showed a substrate preference toward 6-sulfated and 3,4-disulfatedN-acetylglucosamines over non-sulfated and 3-sulfatedN-acetylglucosamines. The purified BbhII directly released 6-sulfatedN-acetylglucosamine from porcine gastric mucin and the expression ofbbhIIwas moderately induced in the presence of mucin. This de-capping activity may promote utilization of sulfated glycans of mucin by other bacteria including bifidobacteria, thereby establishing the symbiotic relationship between human and gut microbes. BbhII encodes a sulfoglycosidase which is involved in the mucin degradation pathway ofBifidobacterium bifidum.
- Subjects
BIFIDOBACTERIUM bifidum; MUCINS; CARBOHYDRATE metabolism
- Publication
Bioscience, Biotechnology & Biochemistry, 2017, Vol 81, Issue 10, p2018
- ISSN
0916-8451
- Publication type
Article
- DOI
10.1080/09168451.2017.1361810