Characterization and comparison of milk fat globule membrane N-glycoproteomes from human and bovine colostrum and mature milk

Human and bovine milk fat globule membrane (MFGM) proteins have been identified and characterized; however, their glycosylation during lactation remains unclear. We adopted a glycoproteomicsapproach to profile and compare MFGM N- glycoproteomesin human and bovine milk during lactation. A total of 843, 718, 614, and 273 N-glycosite peptides corresponding to 465, 423, 334, and 176 glycoproteinswere identified in human colostrum, human mature milk, bovine colostrum, and bovine mature milk, respectively. The biological functionsof these MFGM N- glycoproteinswere revealed through bioinformatics. Substantial differences were observed between human and bovine milk, and immune-related MFGM N- glycoproteinsvaried between colostrumand mature milk from both species. Our results expand current knowledge of MFGM N- glycoproteomes, and further demonstrate the complexity and biological functionsof MFGM N-glycosylation. These data can provide references for the application of bovine MFGM N- glycoproteinsin infant formulato resemble human milk and in functional foods.