scholarly journals Sharing of human milk oligosaccharides degradants within bifidobacterial communities in faecal cultures supplemented with Bifidobacterium bifidum

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Aina Gotoh ◽  
Toshihiko Katoh ◽  
Mikiyasu Sakanaka ◽  
Yiwei Ling ◽  
Chihaya Yamada ◽  
...  
Keyword(s):  
Human Milk ◽  
Bifidobacterium Bifidum ◽  
Human Milk Oligosaccharides ◽  
Milk Oligosaccharides

scholarly journals Bifidobacterium bifidum Lacto-N-Biosidase, a Critical Enzyme for the Degradation of Human Milk Oligosaccharides with a Type 1 Structure

2008 ◽  
Vol 74 (13) ◽  
pp. 3996-4004 ◽  
Author(s):  
Jun Wada ◽  
Takuro Ando ◽  
Masashi Kiyohara ◽  
Hisashi Ashida ◽  
Motomitsu Kitaoka ◽  
...  
Keyword(s):  
Human Milk ◽  
Enteric Bacteria ◽  
Bifidobacterium Bifidum ◽  
Glycoside Hydrolase Family ◽  
Carbohydrate Binding ◽  
Amino Acid Residues ◽  
Human Milk Oligosaccharides ◽  
Milk Oligosaccharides ◽  
Hydrolase Family

ABSTRACT Breast-fed infants often have intestinal microbiota dominated by bifidobacteria in contrast to formula-fed infants. We found that several bifidobacterial strains produce a lacto-N-biosidase that liberates lacto-N-biose I (Galβ1,3GlcNAc; type 1 chain) from lacto-N-tetraose (Galβ1,3GlcNAcβ1,3Galβ1,4Glc), which is a major component of human milk oligosaccharides, and subsequently isolated the gene from Bifidobacterium bifidum JCM1254. The gene, designated lnbB, was predicted to encode a protein of 1,112 amino acid residues containing a signal peptide and a membrane anchor at the N and C termini, respectively, and to possess the domain of glycoside hydrolase family 20, carbohydrate binding module 32, and bacterial immunoglobulin-like domain 2, in that order, from the N terminus. The recombinant enzyme showed substrate preference for the unmodified β-linked lacto-N-biose I structure. Lacto-N-biosidase activity was found in several bifidobacterial strains, but not in the other enteric bacteria, such as clostridia, bacteroides, and lactobacilli, under the tested conditions. These results, together with our recent finding of a novel metabolic pathway specific for lacto-N-biose I in bifidobacterial cells, suggest that some of the bifidobacterial strains are highly adapted for utilizing human milk oligosaccharides with a type 1 chain.

scholarly journals Bifidobacterium bifidum Lacto-N-Biosidase, a Critical Enzyme for the Degradation of Human Milk Oligosaccharides with a Type 1 Structure

2009 ◽  
Vol 75 (19) ◽  
pp. 6414-6414
Author(s):  
Jun Wada ◽  
Takuro Ando ◽  
Masashi Kiyohara ◽  
Hisashi Ashida ◽  
Motomitsu Kitaoka ◽  
...  
Keyword(s):  
Human Milk ◽  
Bifidobacterium Bifidum ◽  
Human Milk Oligosaccharides ◽  
Milk Oligosaccharides

scholarly journals Bifidobacterium bifidum Extracellular Sialidase Enhances Adhesion to the Mucosal Surface and Supports Carbohydrate Assimilation

mBio ◽  
2017 ◽  
Vol 8 (5) ◽  
Author(s):  
Keita Nishiyama ◽  
Yuji Yamamoto ◽  
Makoto Sugiyama ◽  
Takashi Takaki ◽  
Tadasu Urashima ◽  
...  
Keyword(s):  
Human Milk ◽  
Type A ◽  
Bifidobacterium Bifidum ◽  
Mucosal Surface ◽  
Blood Type ◽  
Human Milk Oligosaccharides ◽  
Milk Oligosaccharides ◽  
Adhesion Properties ◽  
Mechanistic Basis

ABSTRACT Bifidobacterium is a natural inhabitant of the human gastrointestinal (GI) tract. We studied the role of the extracellular sialidase (SiaBb2, 835 amino acids [aa]) from Bifidobacterium bifidum ATCC 15696 in mucosal surface adhesion and carbohydrate catabolism. Human milk oligosaccharides (HMOs) or porcine mucin oligosaccharides as the sole carbon source enhanced B. bifidum growth. This was impaired in a B. bifidum ATCC 15696 strain harboring a mutation in the siabb2 gene. Mutant cells in early to late exponential growth phase also showed decreased adhesion to human epithelial cells and porcine mucin relative to the wild-type strain. These results indicate that SiaBb2 removes sialic acid from HMOs and mucin for metabolic purposes and may promote bifidobacterial adhesion to the mucosal surface. To further characterize SiaBb2-mediated bacterial adhesion, we examined the binding of His-tagged recombinant SiaBb2 peptide to colonic mucins and found that His-SiaBb2 as well as a conserved sialidase domain peptide (aa 187 to 553, His-Sia) bound to porcine mucin and murine colonic sections. A glycoarray assay revealed that His-Sia bound to the α2,6-linked but not to the α2,3-linked sialic acid on sialyloligosaccharide and blood type A antigen [GalNAcα1-3(Fucα1-2)Galβ] at the nonreducing termini of sugar chains. These results suggest that the sialidase domain of SiaBb2 is responsible for this interaction and that the protein recognizes two distinct carbohydrate structures. Thus, SiaBb2 may be involved in Bifidobacterium-mucosal surface interactions as well as in the assimilation of a variety of sialylated carbohydrates. IMPORTANCE Adhesion to the host mucosal surface and carbohydrate assimilation are important for bifidobacterium colonization and survival in the host gastrointestinal tract. In this study, we investigated the mechanistic basis for B. bifidum extracellular sialidase (SiaBb2)-mediated adhesion. SiaBb2 cleaved sialyl-human milk oligosaccharides and mucin glycans to produce oligosaccharides that supported B. bifidum growth. Moreover, SiaBb2 enhanced B. bifidum adhesion to mucosal surfaces via specific interactions with the α2,6 linkage of sialyloligosaccharide and blood type A antigen on mucin carbohydrates. These findings provide insight into the bifunctional role of SiaBb2 and the adhesion properties of B. bifidum strains. IMPORTANCE Adhesion to the host mucosal surface and carbohydrate assimilation are important for bifidobacterium colonization and survival in the host gastrointestinal tract. In this study, we investigated the mechanistic basis for B. bifidum extracellular sialidase (SiaBb2)-mediated adhesion. SiaBb2 cleaved sialyl-human milk oligosaccharides and mucin glycans to produce oligosaccharides that supported B. bifidum growth. Moreover, SiaBb2 enhanced B. bifidum adhesion to mucosal surfaces via specific interactions with the α2,6 linkage of sialyloligosaccharide and blood type A antigen on mucin carbohydrates. These findings provide insight into the bifunctional role of SiaBb2 and the adhesion properties of B. bifidum strains.

scholarly journals Effects of Different Human Milk Oligosaccharides on Growth of Bifidobacteria in Monoculture and Co-culture With Faecalibacterium prausnitzii

2020 ◽  
Vol 11 ◽  
Author(s):  
Lianghui Cheng ◽  
Mensiena B. G. Kiewiet ◽  
Madelon J. Logtenberg ◽  
Andre Groeneveld ◽  
Arjen Nauta ◽  
...  
Keyword(s):  
Human Milk ◽  
Human Milk Oligosaccharides ◽  
Milk Oligosaccharides ◽  
Faecalibacterium Prausnitzii

scholarly journals Regulation of hBD-2, hBD-3, hCAP18/LL37, and Proinflammatory Cytokine Secretion by Human Milk Oligosaccharides in an Organotypic Oral Mucosal Model

Pathogens ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 739
Author(s):  
Ulvi K. Gürsoy ◽  
Krista Salli ◽  
Eva Söderling ◽  
Mervi Gürsoy ◽  
Johanna Hirvonen ◽  
...  
Keyword(s):  
Human Milk ◽  
Expression Profiles ◽  
Three Dimensional ◽  
Human Milk Oligosaccharides ◽  
Proinflammatory Response ◽  
Milk Oligosaccharides ◽  
Culture Model ◽  
Gingival Cells ◽  
Mucosal Secretion ◽  
Immunomodulatory Potential

Human milk oligosaccharides (HMOs), the third largest solid fraction in human milk, can modulate inflammation through Toll-like receptor signaling, but little is known about their immunomodulatory potential in the oral cavity. In this study, we determined whether the HMOs 2’-fucosyllactose (2’-FL) and 3-fucosyllactose (3-FL) regulate human-beta defensin (hBD)-2 and -3, cathelicidin (hCAP18/LL-37), and cytokine responses in human gingival cells using a three-dimensional oral mucosal culture model. The model was incubated with 0.1% or 1% 2’-FL and 3-FL, alone and in combination, for 5 or 24 h, and hBD-2, hBD-3, and hCAP18/LL-37 were analyzed by immunohistochemistry. The expression profiles of interleukin (IL)-1, IL-1RA, IL-8, and monocyte chemoattractant protein (MCP)-1 were determined by LUMINEX immunoassay. The combination of 1% 2’-FL and 1% 3-FL, and 1% 3-FL alone, for 24 h upregulated hBD-2 protein expression significantly (p < 0.001 and p = 0.016, respectively). No changes in the other antimicrobial peptides or proinflammatory cytokines were observed. Thus, 3-FL, alone and in combination with 2´-FL, stimulates oral mucosal secretion of hBD-2, without effecting a proinflammatory response when studied in an oral mucosal culture model.

scholarly journals Rapid capillary gel electrophoresis analysis of human milk oligosaccharides for food additive manufacturing in-process control

2021 ◽  
Author(s):  
Marton Szigeti ◽  
Agnes Meszaros-Matwiejuk ◽  
Dora Molnar-Gabor ◽  
Andras Guttman
Keyword(s):  
Additive Manufacturing ◽  
Process Control ◽  
Human Milk ◽  
Gel Electrophoresis ◽  
Process Analysis ◽  
Food Additive ◽  
Human Milk Oligosaccharides ◽  
Milk Oligosaccharides ◽  
Capillary Gel Electrophoresis

AbstractIndustrial production of human milk oligosaccharides (HMOs) represents a recently growing interest since they serve as key ingredients in baby formulas and are also utilized as dietary supplements for all age groups. Despite their short oligosaccharide chain lengths, HMO analysis is challenging due to extensive positional and linkage variations. Capillary gel electrophoresis primarily separates analyte molecules based on their hydrodynamic volume to charge ratios, thus, offers excellent resolution for most of such otherwise difficult-to-separate isomers. In this work, two commercially available gel compositions were evaluated on the analysis of a mixture of ten synthetic HMOs. The relevant respective separation matrices were then applied to selected analytical in-process control examples. The conventionally used carbohydrate separation matrix was applied for the in-process analysis of bacteria-mediated production of 3-fucosyllactose, lacto-N-tetraose, and lacto-N-neotetraose. The other example showed the suitability of the method for the in vivo in-process control of a shake flask and fermentation approach of 2′-fucosyllactose production. In this latter instance, borate complexation was utilized to efficiently separate the 2′- and 3-fucosylated lactose positional isomers. In all instances, the analysis of the HMOs of interest required only a couple of minutes with high resolution and excellent migration time and peak area reproducibility (average RSD 0.26% and 3.56%, respectively), features representing high importance in food additive manufacturing in-process control. Graphical abstract

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