食品科学 ›› 2025, Vol. 46 ›› Issue (17): 1-13.doi: 10.7506/spkx1002-6630-20250124-188

• 基础研究 •    

基于非标记定量技术的驼乳与牛乳N-糖蛋白质组学比较分析

李丹蕾,孔夏冰,于悦,胡谦,张九凯,陈颖   

  1. (1.北京工商大学食品与健康学院,北京 100048;2.中国检验检疫科学研究院,北京 100176;3.国家市场监督管理总局重点实验室(食品真实性鉴别),北京 100176)
  • 发布日期:2025-08-18
  • 基金资助:
    “十四五”国家重点研发计划重点专项(2022YFD1600103);新疆维吾尔自治区重大科技专项(2022A02006-3)

Label-Free Quantitative Comparison of N-Glycoproteomics between Camel and Cow Milk

LI Danlei, KONG Xiabing, YU Yue, HU Qian, ZHANG Jiukai, CHEN Ying   

  1. (1. School of Food and Health, Beijing Technology and Business University, Beijing 100048, China;2. Chinese Academy of Inspection and Quarantine, Beijing 100176, China;3. Key Laboratory of Food Authenticity Identification, State Administration for Market Regulation, Beijing 100176, China)
  • Published:2025-08-18

摘要: 为深入对比驼乳和牛乳中N-糖蛋白的差异特征,采用非标记定量N-糖蛋白质组学技术,详细比较分析两种乳品中N-糖蛋白的组成及其N-糖基化位点的数量,并利用生物信息学分析了两种乳品N-糖蛋白潜在的生物学功能。驼乳中鉴定出137 个N-糖蛋白和224 个N-糖基化位点;牛乳鉴定出116 个N-糖蛋白和183 个N-糖基化位点。相较于牛乳,驼乳含有更丰富的N-糖蛋白和N-糖基化位点。在鉴定到的N-糖蛋白中,大多数仅具有1 个N-糖基化位点,少数糖蛋白的糖基化程度较高。基因本体论富集分析表明,差异表达的N-糖蛋白主要分布在细胞外区域和细胞外间隙,包含在免疫应答中发挥着重要作用的N-糖蛋白,涉及酶活性、细胞外基质构建、结合作用和信号传导。京都基因与基因组百科全书富集分析显示,差异表达的N-糖蛋白中主要富集于补体和凝血级联反应、溶酶体等代谢通路。上述研究结果为全面解析牛乳和驼乳的糖蛋白组成及糖基化修饰差异提供了科学依据。

关键词: 驼乳;牛乳;N-糖蛋白质组学;糖蛋白;N-糖基化位点;差异比较

Abstract: To understand the differential N-glycoprotein characteristics of camel versus cow milk, we employed label-free quantitative N-glycoproteomics to compare the N-glycoprotein composition and the number of N-glycosylation sites between the two milks and utilized bioinformatics tools to predict potential biological functions of their N-glycoproteins. A total of 137 N-glycoproteins harboring 224 N-glycosylation sites were identified in camel milk, and 116 N-glycoproteins with 183 N-glycosylation sites in cow milk. Compared with cow milk, camel milk exhibited greater diversity in both N-glycoprotein types and N-glycosylation site number. Most identified N-glycoproteins contained only one N-glycosylation site, with only a minority displaying hyperglycosylation. Gene ontology (GO) enrichment analysis revealed that differentially expressed N-glycoproteins were predominantly localized in the extracellular region and extracellular space and played an important role in immune response involving enzymatic activity, extracellular matrix organization, molecular binding, and signal transduction. Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analysis indicated that these proteins were mainly enriched in metabolic processes such as complement and coagulation cascades and lysosomal pathways. Collectively, these findings provide molecular-level insights into the differences in N-glycoprotein composition and glycosylation between cow and camel milk.

Key words: camel milk; cow milk; N-glycoproteomics; glycoprotein; N-glycosylation site; difference comparison

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