Glycosylation in Drosophila S2 cells

IF 3.5 2区生物学 Q2 BIOTECHNOLOGY & APPLIED MICROBIOLOGY

Biotechnology and Bioengineering Pub Date : 2024-08-14 DOI:10.1002/bit.28827

Tingting Xu, Lixiang Tong, Zhifu Zhang, Hairong Zhou, Peilin Zheng

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Abstract

In recent years, there has been a remarkable surge in the approval of therapeutic protein drugs, particularly recombinant glycoproteins. Drosophila melanogaster S2 cells have become an appealing platform for the production of recombinant proteins due to their simplicity and low cost in cell culture. However, a significant limitation associated with using the S2 cell expression system is its propensity to introduce simple paucimannosidic glycosylation structures, which differs from that in the mammalian expression system. It is well established that the glycosylation patterns of glycoproteins have a profound impact on the physicochemical properties, bioactivity, and immunogenicity. Therefore, understanding the mechanisms behind these glycosylation modifications and implementing measures to address it has become a subject of considerable interest. This review aims to comprehensively summarize recent advancements in glycosylation modification in S2 cells, with a particular focus on comparing the glycosylation patterns among S2, other insect cells, and mammalian cells, as well as developing strategies for altering the glycosylation patterns of recombinant glycoproteins.

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果蝇 S2 细胞中的糖基化。

近年来，治疗性蛋白质药物，尤其是重组糖蛋白的批准数量激增。黑腹果蝇 S2 细胞因其细胞培养简单、成本低廉，已成为生产重组蛋白质的一个极具吸引力的平台。然而，使用 S2 细胞表达系统的一个重要限制是，它容易引入简单的白甘露糖基化结构，这与哺乳动物表达系统不同。糖蛋白的糖基化模式对其理化性质、生物活性和免疫原性有深远影响，这一点已得到公认。因此，了解这些糖基化修饰背后的机制并采取措施加以解决已成为人们相当感兴趣的话题。本综述旨在全面总结 S2 细胞糖基化修饰的最新进展，尤其侧重于比较 S2、其他昆虫细胞和哺乳动物细胞的糖基化模式，以及开发改变重组糖蛋白糖基化模式的策略。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Biotechnology and Bioengineering 工程技术-生物工程与应用微生物

CiteScore

7.90

自引率

5.30%

发文量

280

审稿时长

2.1 months

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