Lacto-<i>N</i>-Tetraose, Fucosylation, and Secretor Status Are Highly Variable in Human Milk Oligosaccharides From Women Delivering Preterm

Leoz, Maria Lorna A. De; Gaerlan, Stephanie C.; Strum, John S.; Dimapasoc, Lauren M.; Mirmiran, M.; Tancredi, Daniel J.; Smilowitz, Jennifer T.; Kalanetra, Karen M.; Mills, David A.; German, J. Bruce; Lebrilla, Carlito B.; Underwood, Mark A.

doi:10.1021/pr3004979

Cited by 133 publications

(160 citation statements)

References 58 publications

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“…However, the expression of UEA-reactive glycotopes in human milk AGP varied among individuals as a result of the nonsecretor status of mothers who do not express (or express in minute amounts) a1,2-fucosylglycotopes in their milk or other body secretions. 30,31 In our randomized study, 19% (n = 24) of milk samples did not react with UEA, and we assumed that they were from nonsecretors, so that those samples were excluded from the statistical analysis. The expression of a1,3-fucosylated glycotopes had quite a different profile than those of other terminally located sugar structures: its relative amount was low in colostrums and significantly higher in transitional and mature milk (Table 1).…”

Section: Discussionmentioning

confidence: 99%

“…Although according to Froehlich et al 2 there is no common pattern for the alterations of particular milk glycoproteins during lactation, the sialylation and fucosylation changes are more or less similar to those of third-trimester amniotic AGP, 14,15 other milk glycoproteins, 7,8 and abundantly present HMOs. 4,30,31 It seems likely that the same set of glycosyltransferases is involved in elongation and branching of glycans of glycoconjugates and HMOs in lactating mammary glands. 3,4,33 Additionally, hormones, especially at the hormone target organs, such as the mammary gland, can affect the local synthesis 34 and glycosylation of glycoproteins.…”

Section: Discussionmentioning

confidence: 99%

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Lactation Stage-Related Expression of Sialylated and Fucosylated Glycotopes of Human Milk α-1-Acid Glycoprotein

Orczyk-Pawiłowicz

Hirnle

Berghausen-Mazur

et al. 2014

Breastfeeding Medicine

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Background: Because terminal sugars of a-1-acid glycoprotein (AGP) are reported to be involved in antiinflammatory and immunomodulatory processes, their expressions might have an influence on the proper function of immune system of newborns. Here, relative amounts of sialylated and fucosylated glycotopes on human milk AGP over normal lactation were investigated. Materials and Methods: AGP concentration and relative amounts of its sialylated and fucosylated glycovariants were analyzed in early colostrum, colostrum, and transitional and mature milk samples of 127 healthy mothers by lectin-AGP enzyme-linked immunosorbent assay using a2,3-and a2,6-sialic acid and a1,2-, a1,3-, and a1,6-fucose specific biotinylated Maackia amurensis, Sambucus nigra, Ulex europaeus, Tetragonolobus purpureus, and Lens culinaris lectins, respectively. Results: AGP concentration in human milk was about 30 times lower than in plasma of lactating mothers and decreased gradually over lactation. Milk AGP showed significantly higher expression of sialylated and fucosylated glycotopes in comparison with those of plasma AGP. Milk AGP glycovariants containing a2,6-sialylated and a1,6-and a1,2-fucosylated glycotopes showed the highest relative amounts in early colostrums. With progression of lactation, the expressions of glycotopes a1,2-fucosylated decreased starting from Day 4 and those of a2,6-sialylated and a1,6-fucosylated from Day 8 of lactation, whereas the level of a2,3-sialyl-glycotope was almost constant over 45 days of lactation. In contrast, the expression of a1,3-linked fucose on AGP was low in colostrums and significantly higher in transitional and mature milk. Conclusions: The relative amounts of sialylated and fucosylated glycovariants of human hindmilk AGP significantly varied between Days 2 and 45 of normal lactation.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Lactation Stage-Related Expression of Sialylated and Fucosylated Glycotopes of Human Milk α-1-Acid Glycoprotein

Orczyk-Pawiłowicz

Hirnle

Berghausen-Mazur

et al. 2014

Breastfeeding Medicine

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“…Significant differences exist in HMO abundance and composition among different mothers and across lactation stages (Coppa et al, 1999;De Leoz et al, 2012;Niñonuevo et al, 2008). An important association also exists between HMO and the blood group type of the mother represented by the Lewis system and the secretor genes, which generates four different groups of milks (Totten et al, 2012).…”

Section: Structures Of Hmomentioning

confidence: 99%

Consumption of human milk glycoconjugates by infant-associated bifidobacteria: mechanisms and implications

2013

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Human milk is a rich source of nutrients and energy, shaped by mammalian evolution to provide all the nutritive requirements of the newborn. In addition, several molecules in breast milk act as bioactive agents, playing an important role in infant protection and guiding a proper development. While major breast milk nutrients such as lactose, lipids and proteins are readily digested and consumed by the infant, other molecules, such as human milk oligosaccharides and glycosylated proteins and lipids, can escape intestinal digestion and transit through the gastrointestinal tract. In this environment, these molecules guide the composition of the developing infant intestinal microbiota by preventing the colonization of enteric pathogens and providing carbon and nitrogen sources for other colonic commensals. Only a few bacteria, in particular Bifidobacterium species, can gain access to the energetic content of milk as it is displayed in the colon, probably contributing to their predominance in the intestinal microbiota in the first year of life. Bifidobacteria deploy exquisite molecular mechanisms to utilize human milk oligosaccharides, and recent evidence indicates that their activities also target other human milk glycoconjugates. Here, we review advances in our understanding of how these microbes have been shaped by breast milk components and the strategies associated with their consumption of milk glycoconjugates.

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“…In more complex HMO, the lactose core is conjugated with repeats of lacto-N-biose I (Gal␤1-3GlcNAc; LNB; type 1 chain) or N-acetyllactosamine (Gal␤1-4GlcNAc; type 2 chain), producing molecules with a degree of polymerization larger than 4 (4). These core structures can be modified by fucose and sialic acid residues via different linkages, with fucosylated neutral oligosaccharides the most representative in human milk (5). Although a large number of different HMO structures have been determined, a few isomers can represent up to 70% of the total molecules (6).…”

mentioning

confidence: 99%

Variation in Consumption of Human Milk Oligosaccharides by Infant Gut-Associated Strains of Bifidobacterium breve

Ruíz-Moyano¹,

Totten

Garrido

et al. 2013

Appl Environ Microbiol

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215

210

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Human milk contains a high concentration of complex oligosaccharides that influence the composition of the intestinal microbiota in breast-fed infants. Previous studies have indicated that select species such as Bifidobacterium longum subsp. infantis and Bifidobacterium bifidum can utilize human milk oligosaccharides (HMO) in vitro as the sole carbon source, while the relatively few B. longum subsp. longum and Bifidobacterium breve isolates tested appear less adapted to these substrates. Considering the high frequency at which B. breve is isolated from breast-fed infant feces, we postulated that some B. breve strains can more vigorously consume HMO and thus are enriched in the breast-fed infant gastrointestinal tract. To examine this, a number of B. breve isolates from breast-fed infant feces were characterized for the presence of different glycosyl hydrolases that participate in HMO utilization, as well as by their ability to grow on HMO or specific HMO species such as lacto-N-tetraose (LNT) and fucosyllactose. All B. breve strains showed high levels of growth on LNT and lacto-N-neotetraose (LNnT), and, in general, growth on total HMO was moderate for most of the strains, with several strain differences. Growth and consumption of fucosylated HMO were strain dependent, mostly in isolates possessing a glycosyl hydrolase family 29 ␣-fucosidase. Glycoprofiling of the spent supernatant after HMO fermentation by select strains revealed that all B. breve strains can utilize sialylated HMO to a certain extent, especially sialyl-lacto-N-tetraose. Interestingly, this specific oligosaccharide was depleted before neutral LNT by strain SC95. In aggregate, this work indicates that the HMO consumption phenotype in B. breve is variable; however, some strains display specific adaptations to these substrates, enabling more vigorous consumption of fucosylated and sialylated HMO. These results provide a rationale for the predominance of this species in breast-fed infant feces and contribute to a more accurate picture of the ecology of the developing infant intestinal microbiota.

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Lacto-N-Tetraose, Fucosylation, and Secretor Status Are Highly Variable in Human Milk Oligosaccharides From Women Delivering Preterm

Cited by 133 publications

References 58 publications

Lactation Stage-Related Expression of Sialylated and Fucosylated Glycotopes of Human Milk α-1-Acid Glycoprotein

Lactation Stage-Related Expression of Sialylated and Fucosylated Glycotopes of Human Milk α-1-Acid Glycoprotein

Consumption of human milk glycoconjugates by infant-associated bifidobacteria: mechanisms and implications

Variation in Consumption of Human Milk Oligosaccharides by Infant Gut-Associated Strains of Bifidobacterium breve

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