RRC ID 50968
著者 Katoh T, Maeshibu T, Kikkawa KI, Gotoh A, Tomabechi Y, Nakamura M, Liao WH, Yamaguchi M, Ashida H, Yamamoto K, Katayama T.
タイトル Identification and characterization of a sulfoglycosidase from Bifidobacterium bifidum implicated in mucin glycan utilization.
ジャーナル Biosci Biotechnol Biochem
Abstract Human gut symbiont bifidobacteria possess carbohydrate-degrading enzymes that act on the O-linked glycans of intestinal mucins to utilize those carbohydrates as carbon sources. However, our knowledge about mucin type O-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 several Bifidobacterium strains to degrade a sulfated glycan substrate and identified a 6-sulfo-β-d-N-acetylglucosaminidase, also termed sulfoglycosidase, encoded by bbhII from Bifidobacterium bifidum JCM 7004. A recombinant BbhII protein showed a substrate preference toward 6-sulfated and 3,4-disulfated N-acetylglucosamines over non-sulfated and 3-sulfated N-acetylglucosamines. The purified BbhII directly released 6-sulfated N-acetylglucosamine from porcine gastric mucin and the expression of bbhII was 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.
巻・号 81(10)
ページ 2018-2027
公開日 2017-10-1
DOI 10.1080/09168451.2017.1361810
PMID 28814130
MeSH Acetylglucosaminidase / chemistry Acetylglucosaminidase / genetics Acetylglucosaminidase / metabolism* Amino Acid Sequence Bifidobacterium bifidum / enzymology* Bifidobacterium bifidum / genetics Bifidobacterium bifidum / metabolism Gene Expression Regulation, Bacterial Mucins / metabolism* Polysaccharides / metabolism*
IF 1.516
引用数 9
リソース情報
一般微生物 JCM 7004 JCM 1254