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Characterisation and comparison site-specific N-glycosylation of whey proteins from donkey and human colostrum and mature milk using glycoproteomics

ABSTRACT: Although the composition of donkey milk is similar to that of human milk, systematic comparisons of the site-specific N-glycosylation patterns of their whey proteins are lacking. In this study, hydrophilic interaction chromatography-based enrichment of intact N-glycopeptides, coupled with a site-specific glycoproteomics strategy, was used to systematically characterise whey N-glycoproteins in donkey colostrum (DC), donkey mature milk (DM), human colostrum (HC), and human mature milk (HM) for the first time. We identified 628, 347, 868, and 425 site-specific N-glycans mapped to 135, 67, 113, and 60 glycoproteins in DC, DM, HC, and HM, respectively. Bioinformatic analysis revealed the potential biological effects of N-glycosylation modifications on the whey proteins themselves. Our findings elucidated the composition of donkey and human milk whey N-glycoproteins and their potential structure-activity relationships and provided guidance for the production of specific functional donkey milk products and the development of donkey milk-based infant formulas.

ORGANISM(S): Homo Sapiens Equus Caballus

SUBMITTER: Xiqing Yue

PROVIDER: PXD050759 | iProX | Tue Mar 19 00:00:00 GMT 2024

REPOSITORIES: iProX

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Project description:The objective of the present study was to examine the proteome dynamics of somatic cells from colostrum to mature milk. Milk somatic cells are a mixture of mammary epithelial cells (MECs) and immune cells, secreted in milk during milking. Besides protecting the mammary gland, the milk somatic cells have a dual role of contributing to the newborn calf’s health and development and it is unclear how their cargo is altered during the initiation of lactation. Somatic cells were isolated by density gradient centrifugation method from milk obtained from buffaloes on postpartum day 1 (D1; colostrum), 4 (D4; early transitional), 7 (D7; late transitional), and 15 (D15; mature). Quantitative proteomic analysis by liquid chromatography-tandem mass spectrometry (LC-MS/ MS) of homogenate D1, D4, D7, and D15 (n = 6), identified a total of 4429 proteins. 71 proteins were uniquely expressed on D1, while 10, 25 and 15 unique proteins respectively on D4, D7 and D15. Of the high-confidence proteins, 3949 were common among all 4 days of lactation. The significantly changed proteins from the colostrum to mature milk were analyzed using gene ontology enrichment and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways, and their interactions were generated using the Search Tool for Retrieval of Interacting Genes/Proteins (STRING) database. Results indicated the up-regulated proteins across the days were involved in metabolic processes like PPAR signaling, biosynthesis of lipids, amino acids and cofactors, amino and nucleotide sugar metabolism, glycolysis, and peroxisome. The down-regulated proteins were involved in phospholipid efflux and triglyceride (TG) homeostasis, electrolyte balance, mineral absorption and associated hormone regulation, complement and coagulation cascades, and immune-related functions like negative regulation of cytokine production, antigen processing and presentation, and mRNA processing, etc. Our study provides comprehensive alterations in the milk somatic cell proteome. In conclusion, the changes in biological functions indicate both mammary function/metabolism and the specific developmental requirements during the initial phases of calf development.

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Characterisation and comparison site-specific N-glycosylation of whey proteins from donkey and human colostrum and mature milk using glycoproteomics

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