Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins

Katayama, Takane; Fujita, Kiyotaka; Yamamoto, Kenji

doi:10.1263/jbb.99.457

Cited by 71 publications

(56 citation statements)

References 41 publications

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“…Given the diversity and complexity of mucin structures found within the gut (12,29), specific strategies for deconstructing these molecules must be inherent features in the genomes of mucinusing bacteria. The B. bifidum PRL2010 genome encodes various glycosyl hydrolases putatively implicated in degradation of mucinderived oligosaccharides, including a predicted cell wall-anchored endo-α-N-acetylgalactosaminidase (BBPR_0264), an enzyme that has been shown previously to catalyze the hydrolysis of the O-glycosidic α-linkage between GalNAc and serine/threonine residues of various mucin-type glycoproteins (30)(31)(32). Moreover, the genome of B. bifidum PRL2010 encodes a putative 1,2-α-Lfucosidase (BBPR_0193), as well as a predicted 1,3/4-α-L-fucosidase (BBPR_1360), which releases various α-linked L-fucoses from the oligosaccharide core of the mucin structure (33)(34)(35).…”

Section: Resultsmentioning

confidence: 99%

Genome analysis of Bifidobacterium bifidum PRL2010 reveals metabolic pathways for host-derived glycan foraging

Turroni

Bottacini²,

Foroni³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

321

373

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The human intestine is densely populated by a microbial consortium whose metabolic activities are influenced by, among others, bifidobacteria. However, the genetic basis of adaptation of bifidobacteria to the human gut is poorly understood. Analysis of the 2,214,650-bp genome of Bifidobacterium bifidum PRL2010, a strain isolated from infant stool, revealed a nutrient-acquisition strategy that targets host-derived glycans, such as those present in mucin. Proteome and transcriptome profiling revealed a set of chromosomal loci responsible for mucin metabolism that appear to be under common transcriptional control and with predicted functions that allow degradation of various O-linked glycans in mucin. Conservation of the latter gene clusters in various B. bifidum strains supports the notion that host-derived glycan catabolism is an important colonization factor for B. bifidum with concomitant impact on intestinal microbiota ecology.coevolution | genomics | host-glycans metabolism | human gut intestinal bacteria | mucin

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Section: Resultsmentioning

confidence: 99%

Genome analysis of Bifidobacterium bifidum PRL2010 reveals metabolic pathways for host-derived glycan foraging

Turroni

Bottacini²,

Foroni³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

321

373

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“…We focused on the unique sugar catabolic pathway of bifidobacteria, and have revealed, for the first time, the gene organizations and the primary structures of 1,2 α L fucosidase and endo α N acetylgalactosaminidase, both of which were capable of acting on and degrading naturally occurring substrates. Therefore, these extracellular glycosidases should play significant roles for bifidobacteria in acquiring carbon sources in the lower intestinal tract of humans, 16) which was further substantiated by the recent finding of a novel GNB LNB pathway identified in bifidobacteria by Kitaoka et al . 18) As mentioned in the paper of Kitaoka et al ., 17) there are two missing enzymes to be isolated for completely figuring out this pathway; i.e.…”

Section: Concluding Remarks and Future Perspectivementioning

confidence: 87%

Functions of Novel Glycosidases Isolated from Bifidobacteria

Katayama¹,

Wada²,

Fujita³

et al. 2008

J. Appl. Glycosci.

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The genes for 1,2-α-L-fucosidase and endo-α-N-acetylgalactosaminidase have been cloned from Bifidobacterium bifidum JCM1254 and Bifidobacterium longum JCM1217, respectively. The catalytic domain of 1,2-α-L-fucosidase (AfcA) specifically hydrolyzed the terminal α-(1 2)-fucosidic linkages of human milk oligosaccharides and sugar chains of glycoproteins. It exhibited high sequence similarity to several hypothetical proteins in a database, and thus, novel glycoside hydrolase (GH) family 95 has been created. Catalytically important residues of the domain, which were revealed by X-ray crystallographic analysis, were well conserved within the family except for one residue located at the 1 subsite. Endo-α-N -acetylgalactosaminidase (EngBF) that was expressed as C-terminally histidine-tagged protein was found to liberate Galβ1,3GalNAc disaccharide from Core 1-type O-glycans. Its homologues were found in the genomes of several bacteria, and thus a novel GH family (GH101) has been established. Considering that both AfcA and EngBF were able to degrade natural substrates present in intestine, it was envisaged that the enzymes play important roles for the organisms in making their habitats in the colon. The recent finding of the GNB LNB pathway in bifidobacterial cells by Kitaoka s group further supports this notion.

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“…It is theˆrst report of a glycosynthase from an inverting aglycosidase. This enzyme was theˆrst reported to hydrolyze a-1,2-linked L-fucose speciˆcally at the non-reducing end (81,82). No signiˆcant identity in the existing amino acid sequences was detected with any other fucosidases, and the enzyme was classiˆed in a new family, GH95.…”

Section: E Conversion Of Rex Into Glycosynthase E-1 Hehre Resynthesmentioning

confidence: 99%

Conversion of inverting glycoside hydrolases into catalysts for synthesizing glycosides employing a glycosynthase strategy

Kitaoka

Honda

Fushinobu

et al. 2009

TIGG

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23Trends in Glycoscience and Glycotechnology Vol. 21 No. 117 (2009) AbstractReducing-end xylose-releasing exo-oligoxylanase (Rex, EC. 3.2.1.156) is an inverting xylanolytic enzyme, belonging to the glycoside hydrolase (GH) family 8, which hydrolyzes xylooligosaccharides to release xylose (X1) from its reducing end. Rex hydrolyzes a-xylobiosyl ‰uo-ride (a-X2F) to yield xylobiose (X2) only in the presence of X1, conˆrming the Hehre resynthesis-hydrolysis mechanism. A library of mutant Rex at the catalytic base (D263) was constructed by saturation mutagenesis, in which D263C accumulated the highest level of xylotriose (X 3 ) from a-X 2 F and X 1 . However, F -releasing activities of the mutants were much less than that of the wild type. Next, Y198 residue of Rex that forms a hydrogen bond with nucleophilic water was substituted with phenylalanine, causing a marked decrease in hydrolytic activity and a small increase in the F -releasing activity from a-X2F in the presence of X1. Y198F of Rex accumulated more product during the glycosynthase reaction than D263C. Recently, an inverting a-1,2-fucosidase belonging to GH95 was converted into glycosynthase by mutating a catalytic base residue. In both cases, the catalytic base should be intact.

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Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins

Cited by 71 publications

References 41 publications

Genome analysis of Bifidobacterium bifidum PRL2010 reveals metabolic pathways for host-derived glycan foraging

Genome analysis of Bifidobacterium bifidum PRL2010 reveals metabolic pathways for host-derived glycan foraging

Functions of Novel Glycosidases Isolated from Bifidobacteria

Conversion of inverting glycoside hydrolases into catalysts for synthesizing glycosides employing a glycosynthase strategy

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