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Lectin microarray profiling and monosaccharide analysis of bovine milk immunoglobulin G oligosaccharides during the first 10 days of lactation
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2019-04-02
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Feeney S, Gerlach JQ, Slattery H, Kilcoyne M, Hickey RM, Joshi L. Lectin microarray profiling and monosaccharide analysis of bovine milk immunoglobulin G oligosaccharides during the first 10 days of lactation. Food Sci Nutr. 2019 Apr 2;7(5):1564-1572. doi: 10.1002/fsn3.950. PMID: 31139369; PMCID: PMC6526632.
Abstract
Immunoglobulin G (IgG) in bovine milk is credited with ensuring efficient passive immunity for newborn calves. Bovine milk IgG glycosylation may also have positive
impacts on the health of nonbovine consumers of cow's milk. Milk IgG's glycosylation
contributes to effector function and may also protect it from protease digestion, allowing IgG to reach the intestine for absorption. However, relatively little is known
about changes in milk IgG oligosaccharide presentation and composition over early
lactation. In this work, IgG was isolated from milk pooled from three cows at four
time points over the first 10 days of lactation postparturition. Purified IgG was labeled with a fluorescent dye and interrogated with a microarray consisting of 48
carbohydrate-binding proteins (lectins) from plant, fungal, and bacterial sources.
Lectin microarray profiles suggested that only subtle changes in the glycosylation of
IgG occurred during days 2 and 3 of lactation, but by day 10, the lectin profile diverged from the other three time points. Monosaccharide analysis carried out after
hydrolysis confirmed that the ratios of oligosaccharide components remained relatively stable through day 3 and also that sialylation was substantially reduced by day
10. The differences that were observed for glycosylation suggest that different functionalities associated with IgG glycosylation may be required in the first days of life.