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家蚕病毒抗性和敏感品系中 N-和 O-糖蛋白的精确定位。

Precision mapping of N- and O-glycoproteins in viral resistant and susceptible strains of Bombyx mori.

机构信息

Institute of Life Sciences, Jiangsu University, Zhenjiang 212013, China; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China.

Institute of Life Sciences, Jiangsu University, Zhenjiang 212013, China.

出版信息

J Invertebr Pathol. 2019 Oct;167:107250. doi: 10.1016/j.jip.2019.107250. Epub 2019 Sep 18.

DOI:10.1016/j.jip.2019.107250
PMID:31541622
Abstract

Protein glycosylation plays important roles in protein structure, function, and immune recognition, among many other activities. One of the major roles of glycans and glycoconjugates on the cell surface is acting as the receptor for outside pathogens such as viruses. During the initial stage of viral replication, viruses interact with cell membrane receptors, which are in many cases glycoproteins. Identifying such glycoproteins is essential to understanding the mechanisms of viral infection, as well as developing antiviral strategies. Silkworm is an important economic insect as well as a model organism for molecular biology, yet current knowledge on its glycoproteome is far from complete due to both analytical challenges and perceived lack of importance. In this study, we performed a large-scale glycoproteomic survey for two silkworm Bombyx mori strains 306 and NB, which are susceptible and resistant to the baculovirus Bombyx mori nucleopolyhedrovirus (BmNPV), respectively. More than 400 silkworm N- and O- glycoproteins were identified with high confidence, demonstrating that this organism employs extensive glycosylation. We mapped some glycoproteins only to the BmNPV susceptible or resistant strain, underlining the potential relationship between glycosylation and viral susceptibility. We predicted O-glycoproteins and O-glycan compositions for the first time for this organism. The variations in glycan site occupancy, as well as glycan diversity between the two silkworm strains, provide an insight into role of glycosylation in viral recognition and infection processes.

摘要

蛋白质糖基化在蛋白质结构、功能和免疫识别等许多活动中发挥着重要作用。糖链和糖缀合物在细胞表面的主要作用之一是作为细胞外病原体(如病毒)的受体。在病毒复制的初始阶段,病毒与细胞膜受体相互作用,而这些受体在许多情况下是糖蛋白。鉴定这些糖蛋白对于了解病毒感染的机制以及开发抗病毒策略至关重要。家蚕是一种重要的经济昆虫,也是分子生物学的模式生物,但由于分析挑战和感知到的不重要性,目前对其糖蛋白质组的了解还远远不够。在这项研究中,我们对两个家蚕品系 306 和 NB 进行了大规模的糖蛋白质组学调查,这两个品系分别对杆状病毒家蚕核型多角体病毒(BmNPV)敏感和耐受。我们用高可信度鉴定了超过 400 种家蚕 N-和 O-糖蛋白,这表明该生物体广泛采用了糖基化。我们将一些糖蛋白仅映射到 BmNPV 敏感或耐受菌株,这强调了糖基化与病毒易感性之间的潜在关系。我们首次为该生物体预测了 O-糖蛋白和 O-聚糖组成。两种家蚕品系中糖基化位点占有率和聚糖多样性的变化,为糖基化在病毒识别和感染过程中的作用提供了深入的了解。

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引用本文的文献

1
Glycoproteome in silkworm Bombyx mori and alteration by BmCPV infection.家蚕糖蛋白组学及其在 BmCPV 感染中的变化。
J Proteomics. 2020 Jun 30;222:103802. doi: 10.1016/j.jprot.2020.103802. Epub 2020 Apr 29.