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[家蚕微孢子虫极管蛋白1(NbPTP1)在果蝇S2细胞系中的表达及其糖基化]

[Expression of Polar Tube Protein 1 (NbPTP1) from Nosema bombycis in Drosophila S2 cell lines and its glycosylation].

作者信息

Long Mengxian, Tan Yaoyao, Liu Keke, Wu Yujiao, Lü Qing, Pan Guoqing, Zhou Zeyang

机构信息

State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400715, China.

College of Life Sciences, Chongqing Normal University, Chongqing 400047, China.

出版信息

Sheng Wu Gong Cheng Xue Bao. 2018 Sep 25;34(9):1460-1468. doi: 10.13345/j.cjb.170478.

Abstract

The polar tube protein is the major component of polar tube, and can specifically locate on the polar tube of microsporidia and plays an important role in invasion host cell. In this study, we analyzed the potential O- and Nglycosylation sites in polar tube protein 1 from Nosema bombycis. NbPTP1 was successfully cloned to eukaryotic expression vector pMT/Bip/V5-His A, involved V5 and His tags. After transfection, NbPTP1 gene could be efficiently expressed in Drosophila S2 cells. In addition, Lectin blotting and beta elimination analysis showed that NbPTP1 expressed in Drosophila S2 cells was O-glycosylation. These studies provided a basis for understanding the relationship between glycosylation and function of NbPTP1, helped us to reveal the infection mechanism of microsporidia and established effective diagnosis and prevention methods for microsporidia.

摘要

极管蛋白是极管的主要成分,可特异性定位于微孢子虫的极管上,并在入侵宿主细胞中发挥重要作用。在本研究中,我们分析了家蚕微孢子虫极管蛋白1潜在的O-糖基化和N-糖基化位点。NbPTP1成功克隆至真核表达载体pMT/Bip/V5-His A,带有V5和His标签。转染后,NbPTP1基因可在果蝇S2细胞中高效表达。此外,凝集素印迹和β-消除分析表明,在果蝇S2细胞中表达的NbPTP1为O-糖基化。这些研究为理解NbPTP1糖基化与功能之间的关系提供了依据,有助于我们揭示微孢子虫的感染机制,并建立针对微孢子虫的有效诊断和预防方法。

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