Quantitative label-free site-specific glycoproteomic analysis of the milk fat globule membrane protein in human colostrum and mature milk

• Published in: Carbohydrate polymers Vol. 306; p. 120588
• Main Authors: Guan, Boyuan, Zhang, Zhenghan, Liu, Xiaoyu, Zhao, Shanshan, Bai, Xue, Luo, Xue, Feng, Daguang, Yang, Liu, Cao, Xueyan, Yue, Xiqing
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 15.04.2023
• Subjects: Colostrum; Colostrum - chemistry; Colostrum - metabolism; Female; Glycoproteins - chemistry; Human milk; Humans; Infant, Newborn; Mature milk; Membrane Proteins - metabolism; Milk fat globule membrane protein; Milk Proteins - chemistry; Milk, Human - chemistry; Pregnancy; Site-specific glycoproteomics; Tandem Mass Spectrometry; Human milk; Site-specific glycoproteomics; Colostrum; Milk fat globule membrane protein; Mature milk
• ISSN: 0144-8617; 1879-1344
• DOI: 10.1016/j.carbpol.2023.120588

Human milk fat globule membrane (MFGM) proteins, which are N-glycosylated, play essential roles in neonatal development and physiological health. However, the profiles and landscape changes in the site-specific N-glycosylation of human MFGM proteins during lactation remain unclear. Therefore, in this study, based on an intact glycopeptide-centred strategy, 2617 unique site-specific N-glycans of 221 MFGM glycoproteins in human colostrum and 986 unique site-specific N-glycans of 200 MFGM glycoproteins in mature milk were characterised and quantified using label-free glycoproteomics. With milk maturation, 33 site-specific N-glycans on 10 N-glycoproteins increased significantly, and 113 site-specific N-glycans on 25 N-glycoproteins decreased significantly. Moreover, human MFGM glycoproteins with core-α1,6-fucosylated structures and Lewis and sialylated branching structures play a role in the biological processes of antigen processing and presentation. This study reveals the dynamic changes in human MFGM protein N-glycosylation patterns during lactation. Meanwhile, the study deepens our understanding of site-specific N-glycosylation of human MFGM glycoproteins. The results of the study provide a background reference for the development of infant formulas. [Display omitted]