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Profiling temporal changes in bovine milk lactoferrin glycosylation using lectin microarrays
Noelle O'Riordan1, Jared Q Gerlach2, Michelle Kilcoyne2
1Teagasc Food Research Centre, Moorepark, Fermoy, Co. Cork, Ireland; Glycoscience Group, National Centre for Biomedical Engineering Science, National University of Ireland Galway, Galway, Ireland.
Food Chemistry
|July 21, 2014
Summary
Bovine lactoferrin (bLF) structure changes during lactation. Early lactation bLF has more diverse glycans, while later lactation bLF shows more oligomannose structures, suggesting functional differences.
Area of Science:
- Biochemistry
- Glycobiology
- Animal Science
Background:
- Bovine lactoferrin (bLF) is a milk glycoprotein with diverse biological activities.
- The role of bLF's glycans in its function is recognized, but changes during lactation are poorly understood.
Purpose of the Study:
- To investigate the structural changes in bovine lactoferrin (bLF) glycosylation throughout the initial three months of lactation.
- To correlate observed glycan profile differences with potential functional variations in bLF.
Main Methods:
- Isolation of bLF from cow's milk at 13 time points during the first three months of lactation.
- Profiling of bLF glycosylation using lectin microarrays.
- Monosaccharide analysis to identify specific glycan components.
Main Results:
- Significant differences in bLF glycoprofiles were observed between early and late lactation stages.
- N-glycolylneuraminic acid, a non-human sialic acid, was more prevalent in early lactation milk.
- Early lactation bLF exhibited more diverse complex-type oligosaccharides, whereas late lactation bLF showed an abundance of oligomannose glycans.
Conclusions:
- The glycoprofile of bovine lactoferrin (bLF) undergoes significant structural modifications during lactation.
- These glycan changes, particularly the shift from diverse complex structures to oligomannose types, suggest distinct biological functions for bLF in colostrum versus mature milk.

