α-N-Acetylglucosaminidase from Bifidobacterium bifidum specifically hydrolyzes α-linked N-acetylglucosamine at nonreducing terminus of O-glycan on gastric mucin

Shimada, Yoshimi; Watanabe, Yuka; Wakinaka, Takura; Funeno, Yoshihisa; Kubota, Masayuki; Chaiwangsri, Thida; Kurihara, Shin; Yamamoto, Kenji; Katayama, Takane; Ashida, Hisashi

doi:10.1007/s00253-014-6201-x

Cited by 27 publications

(21 citation statements)

References 29 publications

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“…The reports on a GH95 1,2-α-l-fucosidase (AfcA) from B. bifidum JCM 1254 by Katayama et al [56] and a galactose operon containing a gene encoding a GH112 galacto-N-biose (GNB)/LNB phosphorylase from B. longum JCM 1217 by Kitaoka et al [57] were the key findings that revived attention on HMOs by linking them to bifidobacterial biology, long after the first notion, proposed in 1954 by Gauhe et al [58], that milk oligosaccharides serve as a bifidus factor. Since then, using the strain B. bifidum JCM 1254, extensive studies have been carried out and the gene products relevant to the HMO/mucin utilization pathways have been successfully isolated and characterized [26,27,[59][60][61][62][63][64][65][66]. These efforts have illustrated how B. bifidum extracellularly degrades HMOs and mucin O-glycans into smaller sugars by the concerted action of the many cell surface-anchored GHs summarized in Figure 1.…”

Section: Glycoside Hydrolases Involved In the Degradation Of Hmos/mucmentioning

confidence: 99%

“…Furthermore, B. bifidum possesses specific GHs for degrading various glycan epitopes that are frequently found on mucin O-glycans. GH89 α-N-acetylglucosaminidase acts on terminal α-linked GlcNAc linkages attached to gastric mucin O-glycans [59], while GH110 α-galactosidase acts on the blood group antigen B to liberate Gal [64]. Interestingly, B. bifidum does not have a gene encoding GH109 α-N-acetylgalactosaminidase that acts on the blood group antigen A [69].…”

Section: Glycoside Hydrolases Involved In the Degradation Of Hmos/mucmentioning

confidence: 99%

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Enzymatic Adaptation of Bifidobacterium bifidum to Host Glycans, Viewed from Glycoside Hydrolyases and Carbohydrate-Binding Modules

et al. 2020

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Certain species of the genus Bifidobacterium represent human symbionts. Many studies have shown that the establishment of symbiosis with such bifidobacterial species confers various beneficial effects on human health. Among the more than ten (sub)species of human gut-associated Bifidobacterium that have significantly varied genetic characteristics at the species level, Bifidobacterium bifidum is unique in that it is found in the intestines of a wide age group, ranging from infants to adults. This species is likely to have adapted to efficiently degrade host-derived carbohydrate chains, such as human milk oligosaccharides (HMOs) and mucin O-glycans, which enabled the longitudinal colonization of intestines. The ability of this species to assimilate various host glycans can be attributed to the possession of an adequate set of extracellular glycoside hydrolases (GHs). Importantly, the polypeptides of those glycosidases frequently contain carbohydrate-binding modules (CBMs) with deduced affinities to the target glycans, which is also a distinct characteristic of this species among members of human gut-associated bifidobacteria. This review firstly describes the prevalence and distribution of B. bifidum in the human gut and then explains the enzymatic machinery that B. bifidum has developed for host glycan degradation by referring to the functions of GHs and CBMs. Finally, we show the data of co-culture experiments using host-derived glycans as carbon sources, which underpin the interesting altruistic behavior of this species as a cross-feeder.

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Section: Glycoside Hydrolases Involved In the Degradation Of Hmos/mucmentioning

confidence: 99%

Section: Glycoside Hydrolases Involved In the Degradation Of Hmos/mucmentioning

confidence: 99%

Enzymatic Adaptation of Bifidobacterium bifidum to Host Glycans, Viewed from Glycoside Hydrolyases and Carbohydrate-Binding Modules

et al. 2020

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“…The expression of both genes was highly induced in the presence of mucin ( Ruas-Madiedo et al, 2008 ). Moreover, two novel α- N -acetylgalactosaminidases from B. bifidum JCM 1254 have been identified, NagBb ( Kiyohara et al, 2012 ) and AgnB ( Shimada et al, 2014 ). These enzymes exhibit activity against the core structures in mucin O-glycans.…”

Section: Discovering Probiotics With Genetics and Omicsmentioning

confidence: 99%

Discovering probiotic microorganisms: in vitro, in vivo, genetic and omics approaches

et al. 2015

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Over the past decades the food industry has been revolutionized toward the production of functional foods due to an increasing awareness of the consumers on the positive role of food in wellbeing and health. By definition probiotic foods must contain live microorganisms in adequate amounts so as to be beneficial for the consumer’s health. There are numerous probiotic foods marketed today and many probiotic strains are commercially available. However, the question that arises is how to determine the real probiotic potential of microorganisms. This is becoming increasingly important, as even a superficial search of the relevant literature reveals that the number of proclaimed probiotics is growing fast. While the vast majority of probiotic microorganisms are food-related or commensal bacteria that are often regarded as safe, probiotics from other sources are increasingly being reported raising possible regulatory and safety issues. Potential probiotics are selected after in vitro or in vivo assays by evaluating simple traits such as resistance to the acidic conditions of the stomach or bile resistance, or by assessing their impact on complicated host functions such as immune development, metabolic function or gut–brain interaction. While final human clinical trials are considered mandatory for communicating health benefits, rather few strains with positive studies have been able to convince legal authorities with these health claims. Consequently, concern has been raised about the validity of the workflows currently used to characterize probiotics. In this review we will present an overview of the most common assays employed in screening for probiotics, highlighting the potential strengths and limitations of these approaches. Furthermore, we will focus on how the advent of omics technologies has reshaped our understanding of the biology of probiotics, allowing the exploration of novel routes for screening and studying such microorganisms.

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“…infantis, and B. longum subsp. longum-utilize oligosaccharides from breast milk (9)(10)(11)(12)(13)(14)(15)(16)(17)(18) and glycoprotein glycans secreted from the gastrointestinal tract (19)(20)(21)(22). We also reported that B. longum subsp.…”

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confidence: 89%

Two Novel α- l -Arabinofuranosidases from Bifidobacterium longum subsp. longum Belonging to Glycoside Hydrolase Family 43 Cooperatively Degrade Arabinan

Komeno

Hayamizu

Fujita

et al. 2019

Appl Environ Microbiol

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Arabinose-containing poly- or oligosaccharides are suitable carbohydrate sources for Bifidobacterium longum subsp. longum. However, their degradation pathways are poorly understood. In this study, we cloned and characterized the previously uncharacterized glycoside hydrolase family 43 (GH43) enzymes B. longum subsp. longum ArafC (BlArafC; encoded by BLLJ_1852) and B. longum subsp. longum ArafB (BlArafB; encoded by BLLJ_1853) from B. longum subsp. longum JCM 1217. Both enzymes exhibited α-l-arabinofuranosidase activity toward p-nitrophenyl-α-l-arabinofuranoside but no activity toward p-nitrophenyl-β-d-xylopyranoside. The specificities of the two enzymes for l-arabinofuranosyl linkages were different. BlArafC catalyzed the hydrolysis of α1,2- and α1,3-l-arabinofuranosyl linkages found on the side chains of both arabinan and arabinoxylan. It released l-arabinose 100 times faster from arabinan than from arabinoxylan but did not act on arabinogalactan. On the other hand, BlArafB catalyzed the hydrolysis of the α1,5-l-arabinofuranosyl linkage found on the arabinan backbone. It released l-arabinose from arabinan but not from arabinoxylan or arabinogalactan. Coincubation of BlArafC and BlArafB revealed that these two enzymes are able to degrade arabinan in a synergistic manner. Both enzyme activities were suppressed with EDTA treatment, suggesting that they require divalent metal ions. The GH43 domains of BlArafC and BlArafB are classified into GH43 subfamilies 27 and 22, respectively, but show very low similarity (less than 15% identity) with other biochemically characterized members in the corresponding subfamilies. The B. longum subsp. longum strain lacking the GH43 gene cluster that includes BLLJ_1850 to BLLJ_1853 did not grow in arabinan medium, suggesting that BlArafC and BlArafB are important for assimilation of arabinan. IMPORTANCE We identified two novel α-l-arabinofuranosidases, BlArafC and BlArafB, from B. longum subsp. longum JCM 1217, both of which are predicted to be extracellular membrane-bound enzymes. The former specifically acts on α1,2/3-l-arabinofuranosyl linkages, while the latter acts on the α1,5-l-arabinofuranosyl linkage. These enzymes cooperatively degrade arabinan and are required for the efficient growth of bifidobacteria in arabinan-containing medium. The genes encoding these enzymes are located side by side in a gene cluster involved in metabolic pathways for plant-derived polysaccharides, which may confer adaptability in adult intestines.

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α-N-Acetylglucosaminidase from Bifidobacterium bifidum specifically hydrolyzes α-linked N-acetylglucosamine at nonreducing terminus of O-glycan on gastric mucin

Cited by 27 publications

References 29 publications

Enzymatic Adaptation of Bifidobacterium bifidum to Host Glycans, Viewed from Glycoside Hydrolyases and Carbohydrate-Binding Modules

Enzymatic Adaptation of Bifidobacterium bifidum to Host Glycans, Viewed from Glycoside Hydrolyases and Carbohydrate-Binding Modules

Discovering probiotic microorganisms: in vitro, in vivo, genetic and omics approaches

Two Novel α- l -Arabinofuranosidases from Bifidobacterium longum subsp. longum Belonging to Glycoside Hydrolase Family 43 Cooperatively Degrade Arabinan

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