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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Site-Specific Analysis of N-Linked Glycosylation Heterogeneity from Royal Jelly Glycoproteins
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Site-Specific Analysis of N-Linked Glycosylation Heterogeneity from Royal Jelly Glycoproteins

机译：皇家果冻糖蛋白的N-连接糖基化异质性的特异性分析

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摘要

Royal jelly (RJ) is secreted by young worker bees, and it plays key roles in the development and physiological function in honeybees and can improve human health. Although there have been analyses on the glycosylation modification of RJ proteins, none of these methods have been conducted on a site-specific analysis of glycosylation from these glycoproteins. Here, a combined glycomics and glycoproteomics strategy was developed for the site-specific analysis of N-linked glycosylation heterogeneity of RJ glycoproteins. First, global characterization of the N-glycome of RJ was performed using a direct infusion ion trap-sequential mass spectrometry (IT-MSn) method. Second, tryptic glycopeptides were enriched and separated by hydrophilic interaction liquid chromatography-ion trap-sequential mass spectrometry (HILIC-IT-MSn). A total of 50 N-glycopeptides and 30 N-glycans have been site-specific glycosylation profiled in major royal jelly protein 1 (MRJP1) and MRJP2 of RJ for the first time. Eighteen of the identified N-glycans have been structurally characterized by IT-MSn, including oligosaccharide composition, sequence, branching, and linkage. Two N-glycosylation sites (N-177 and N-394), 3 sites (N-145, N-178, and N-92), and 1 site of N-183 were identified in MRJP1, MRJP2, and MRJP3, respectively. There were 18, 17, and 2 N-glycans attached to MRJP1, MRJP2, and MRJP3, respectively. The diversity of N-glycans attached to each single glycosylation site of these glycoproteins confirmed that MRJP1 and MRJP2 heterogeneity was mostly associated with their glycoform populations. Understanding the properties of the site-specific glycosylation heterogeneity of the RJ glycoproteins can be potentially useful for producing a glycoprotein with desirable pharmacokinetic and biological activity.
机译：Royal Jelly（RJ）由年轻工人蜜蜂分泌，它在蜜蜂的开发和生理功能中起着关键作用，可以改善人类健康。尽管已经对RJ蛋白的糖基化修饰进行了分析，但是这些方法中没有任何一种在这些糖蛋白的糖基化的特异性特异性分析中进行。在此，开发了组合的血糖和糖蛋白酶策略用于RJ糖蛋白的N-连接糖基化异质性的特异性特异性分析。首先，使用直接输注离子捕集序列质谱（IT-MSN）方法进行RJ的N-GLYCOM的全局表征。二，通过亲水相互作用液相色谱 - 离子捕集质谱法（HILIC-IT-MSN）富集和分离胰蛋白酶糖肽。总共50个n-glycopeptores和30 n-聚糖是在主要的蜂王浆蛋白1（MRJP1）和RJ的MRJP2中的定位特异性糖基化。所鉴定的N-聚糖的18个已经通过IT-MSN结构表征，包括寡糖组合物，序列，支化和连杆。在MRJP1，MRJP2和MRJP3中鉴定出两个N-糖基化位点（N-177和N-394），3位点（N-145，N-178和N-92）和1位N-183位点。分别有18,17和2个N-Glycans分别附着在MRJP1，MRJP2和MRJP3上。附着于这些糖蛋白的每个糖基化位点的N-聚糖的多样性证实MRJP1和MRJP2的异质性主要与其糖族群相关。理解RJ糖蛋白的特异性糖基化异质性的性质可能是潜在的可用于生产具有所需药代动力学和生物活性的糖蛋白。

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