黑腹果蝇n -聚糖的位点特异性分析

Fei Zhao, Chenyu Jia, Fangyu He, Meiting Hu, Xingyu Guo, Jiaxin Zhang, Xuesong Feng
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摘要

背景:黑腹果蝇是一个被充分研究和高度可处理的遗传模型系统,用于破译各种生物过程的分子机制。虽然糖基化是蛋白质翻译后最关键的修饰之一,但与其他模式生物相比,果蝇对糖基化的理解仍然滞后。方法:采用完整的糖肽分析技术,系统地研究了黑腹果蝇的位点特异性n -聚糖谱。这种方法鉴定了果蝇的聚糖、蛋白质及其糖位点,以及位点特异性糖基化的信息,使我们能够知道哪些聚糖附着在哪些糖基化位点上。结果:果蝇的n -聚糖大部分为高甘露糖型(69.3%),与其他昆虫的报道一致。同时,浓缩的n -聚糖也非常丰富(22.7%),并且大多数是单浓缩的。此外,还鉴定出了24种不同的唾液化聚糖与16种糖蛋白结合,这些糖蛋白主要与发育过程有关。基因本体分析表明,果蝇中n -糖基化蛋白参与轴突引导、n -链糖基化、细胞迁移、细胞扩散和组织发育等多种生物学过程。有趣的是,我们发现7种糖基转移酶和4种糖苷酶被n -糖基化,这表明n -聚糖可能在n -聚糖和糖蛋白的合成和降解中发挥调节作用。结论:据我们所知,这项工作首次全面分析了果蝇的位点特异性n -糖基化,从而为理解昆虫糖基化的生物学功能提供了新的视角。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Site-Specific Profiling of N-Glycans in Drosophila melanogaster
Background: Drosophila melanogaster is a well-studied and highly tractable genetic model system for deciphering the molecular mechanisms underlying various biological processes. Although being one of the most critical post-translational modifications of proteins, the understanding of glycosylation in Drosophila is still lagging behind compared with that of other model organisms. Methods: In this study, we systematically investigated the site-specific N-glycan profile of Drosophila melanogaster using intact glycopeptide analysis technique. This approach identified the glycans, proteins, and their glycosites in Drosophila, as well as information on site-specific glycosylation, which allowed us to know which glycans are attached to which glycosylation sites. Results: The results showed that the majority of N-glycans in Drosophila were high-mannose type (69.3%), consistent with reports in other insects. Meanwhile, fucosylated N-glycans were also highly abundant (22.7%), and the majority of them were mono-fucosylated. In addition, 24 different sialylated glycans attached with 16 glycoproteins were identified, and these proteins were mainly associated with developmental processes. Gene ontology analysis showed that N-glycosylated proteins in Drosophila were involved in multiple biological processes, such as axon guidance, N-linked glycosylation, cell migration, cell spreading, and tissue development. Interestingly, we found that seven glycosyltransferases and four glycosidases were N-glycosylated, which suggested that N-glycans may play a regulatory role in the synthesis and degradation of N-glycans and glycoproteins. Conclusions: To our knowledge, this work represents the first comprehensive analysis of site-specific N-glycosylation in Drosophila, thereby providing new perspectives for the understanding of biological functions of glycosylation in insects.
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