Profiling temporal changes in bovine milk lactoferrin glycosylation using lectin microarrays

O’Riordan, Noelle; Gerlach, Jared Q.; Kilcoyne, Michelle; O’Callaghan, J.R.; Kane, Marian; Hickey, Rita M.; Joshi, Lokesh

doi:10.1016/j.foodchem.2014.05.086

Cited by 25 publications

(37 citation statements)

References 35 publications

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“…11,12,29,31 Additionally, the results obtained using lectinbased methods are reported to be well correlated with mass spectrometry analysis of glycan structures. 16 The observed differences in the reactivities of human milk and plasma AGP with the panel of O-glycan specific lectins (Table 1 and Fig. 1) are closely connected with AGP origin.…”

Section: Discussionmentioning

confidence: 74%

“…The advantage of the present strategy over the mass spectrometry and high-performance liquid chromatography methods preceded by enzymatic release of glycans is that they are a more convenient approach that allows for simultaneous analysis of a large number of samples at different time points bound with variable physiopathological conditions without the need for glycan release prior to analysis. 11,16,30 In particular, binding of lectins to ELISA plate-isolated glycoproteins and other lectin-based methods allow rapid and exhaustive analysis and are useful for detecting even weak interactions due to multivalent glycotope-lectin interactions. 11,12,29,31 Additionally, the results obtained using lectinbased methods are reported to be well correlated with mass spectrometry analysis of glycan structures.…”

Section: Discussionmentioning

confidence: 99%

“…[14][15][16] Moreover, O-glycosylation sites as well as O-glycan structures are tissue specific 17 and differ significantly during inflammation 18 and in cancer. 19,20 Additionally, a wide range of O-glycans of colostrum secretory immunoglobulin A can interact with bacterial adhesins, resulting in blockage of their adhesion to host tissues, and they are considered to be a part of innate immunity.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

O-Glycosylation of α-1-Acid Glycoprotein of Human Milk Is Lactation Stage Related

Orczyk-Pawiłowicz

Berghausen-Mazur

Hirnle

et al. 2015

Breastfeeding Medicine

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Section: Discussionmentioning

confidence: 74%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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O-Glycosylation of α-1-Acid Glycoprotein of Human Milk Is Lactation Stage Related

Orczyk-Pawiłowicz

Berghausen-Mazur

Hirnle

et al. 2015

Breastfeeding Medicine

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“…However, bLF carries only N‐glycans with sugar moieties attached via N‐acetyl glucosamine to the asparagine residues of the protein in the specific amino acid sequence Asn‐X‐Ser/Thr, in which X can be any amino acid except proline . hLF has three potential sites for N‐glycosylation, that is, Asn137, Asn478, Asn623, that are always occupied, whereas bLF has five potential sites, that is, Asn 281, Asn233, Asn368, Asn476, and Asn545 . Four sites are always occupied, whereas Asn281 is glycosylated for approximately 30% in bovine colostrum, but is reduced to 15% in mature milk .…”

Section: Introductionmentioning

confidence: 99%

Dietary N‐Glycans from Bovine Lactoferrin and TLR Modulation

Figueroa-Lozano

Valk-Weeber

Leeuwen

et al. 2018

Molecular Nutrition Food Res

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ScopeBovine lactoferrin (bLF) is an ingredient of food supplements and infant formulas given its antimicrobial and antiviral properties. We modified bLF enzymatically to alter its N‐glycosylation and to isolate the glycan chains. The aims of this study include (1) to evaluate whether such derivates induce responses via pattern recognition receptors namely Toll‐like receptors (TLRs) and (2) to relate those responses to their different glycosylation profiles.Methods and resultsThe unmodified and modified bLF fractions are incubated with reporter cell lines expressing pattern recognition receptors. Afterwards, we screen for TLRs and analyze for nuclear factor kappa—light‐chain enhancer of activated B cells (NF‐κB) activation. Activation of reporter cell lines show that signaling is highly dependent on TLRs. The activation pattern of bLF is reduced with the desialylated form and increased with the demannosylated form. In reporter cells for TLR, bLF activate TLR‐4 and inhibit TLR‐3. The isolated glycans from bLF inhibit TLR‐8. TLR‐2, TLR‐5, TLR‐7, and TLR‐9 are not significantly altered.ConclusionThe profile of glycosylation is key for the biological activity of bLF. By understanding how this affects the human defense responses, the bLF glycan profile can be modified to enhance its immunomodulatory effects when used as a dietary ingredient.

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“…Lactoferrin also exhibits several immunemodulating properties in addition to those better-known irondependent, anti-infective capabilities [92,93]. Differences in these functions, may be strongly influenced by glycosylation patterns, which vary over the course of lactation [94,95]. As changes in protein glycosylation can significantly affect structure and stability, this could lead to changes in predominant function attributed to lactoferrin at different times in lactation.…”

Section: Breast Milk Proteins and Protection From Pathogensmentioning

confidence: 99%

Lactation and Intestinal Microbiota: How Early Diet Shapes the Infant Gut

Goldsmith

O’Sullivan

Smilowitz

et al. 2015

J Mammary Gland Biol Neoplasia

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Breast milk is a multifunctional biofluid that provides nutrients along with highly diverse non-nutritive bioactive components such as antibodies, glycans, bacteria, and immunomodulatory proteins. Research over the past decade has confirmed the essential role of breast milk bioactives in the establishment a healthy intestinal microbiota within the infant. The intestinal microbiota of an exclusively breastfed baby is dominated by several species of Bifidobacteria - the most influential member of which is Bifidobacterium longum subspecies infantis (B. infantis) - and is referred to as the milk-oriented microbiome (MOM). MOM is associated with reduced risk of infection in infancy as well as a reduced risk of certain chronic illnesses in adulthood. Establishment and persistence of MOM is dependent on the selective digestion of complex sugar structures in breast milk that are otherwise indigestible to the infant by B. infantis and its relatives. This review focuses primarily on the influence of breast milk glycans and glycosylated proteins on the development of the intestinal microbiome, and how maternal phenotype may influence the development of MOM providing a framework to understand how variation in diet shapes a protective intestinal microbiome.

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Profiling temporal changes in bovine milk lactoferrin glycosylation using lectin microarrays

Cited by 25 publications

References 35 publications

O-Glycosylation of α-1-Acid Glycoprotein of Human Milk Is Lactation Stage Related

O-Glycosylation of α-1-Acid Glycoprotein of Human Milk Is Lactation Stage Related

Dietary N‐Glycans from Bovine Lactoferrin and TLR Modulation

Lactation and Intestinal Microbiota: How Early Diet Shapes the Infant Gut

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