College of Food Science and Engineering, Gansu Agricultural University, Lanzhou 730070, PR China.
College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, PR China.
J Agric Food Chem. 2024 Oct 23;72(42):23606-23615. doi: 10.1021/acs.jafc.4c04354. Epub 2024 Oct 11.
Whey proteins are N-glycosylated proteins that play important roles in a variety of biological processes including immune defense. However, the N-glycosylation of yak colostrum (YC) and mature milk (YM) whey proteins is unknown. Therefore, this study systematically compared and analyzed YC and YM whey N-glycoproteomes using the 4D label-free technique. We identified 162 glycoproteins, 222 glycosylated peptides, and 234 glycosylation sites in YC and YM, of which 59 glycoproteins were differentially expressed in YC and YM. According to gene ontology annotation and KEGG pathway metabolism analysis, the differentially expressed N-glycoproteins were highly enriched in "cell adhesion", "extracellular region", and "calcium binding", and were mainly involved in the extracellular matrix (ECM)-receptor interaction pathway. The immunity-related N-glycoproteins, such as platelet glycoprotein 4 (CD36) and polymeric immunoglobulin receptor (PIGR), were observed to be different between YC and YM. The results revealed the glycosylation sites, composition, and biological functions of YC and YM whey N-glycoprotein, which supplemented our understanding of the N-glycosylation of yak whey proteins.
乳清蛋白是 N-糖基化蛋白，在包括免疫防御在内的多种生物学过程中发挥重要作用。然而，牦牛初乳（YC）和成熟乳（YM）乳清蛋白的 N-糖基化情况尚不清楚。因此，本研究采用 4D 无标记技术系统比较和分析了 YC 和 YM 乳清 N-糖蛋白组。我们在 YC 和 YM 中分别鉴定出 162 种糖蛋白、222 个糖肽和 234 个糖基化位点，其中 59 种糖蛋白在 YC 和 YM 中差异表达。根据基因本体注释和 KEGG 通路代谢分析，差异表达的 N-糖蛋白在“细胞黏附”、“细胞外区”和“钙结合”中高度富集，主要参与细胞外基质（ECM）-受体相互作用通路。观察到 YC 和 YM 之间的免疫相关 N-糖蛋白，如血小板糖蛋白 4（CD36）和多免疫球蛋白受体（PIGR）存在差异。研究结果揭示了 YC 和 YM 乳清 N-糖蛋白的糖基化位点、组成和生物学功能，补充了我们对牦牛乳清蛋白 N-糖基化的认识。
