Department of Chemical Engineering, The Johns Hopkins University, 21218-2694, Baltimore, Maryland, U.S.A..
Cytotechnology. 1996 Jan;20(1-3):149-59. doi: 10.1007/BF00350396.
The BEVS has become widely utilized for production of recombinant proteins. However, protein aggregation and inefficient processing often limit yields, especially for secreted and membrane proteins. Since many proteins of pharmaceutical interest require similar posttranslational processing steps, engineering the folding, assembly, and secretion pathway may enhance the production of a wide variety of valuable complex proteins. Efforts should be undertaken to coexpress the relevant chaperones or foldases at low levels in concert with the final product to ensure the ideal folding and assembly environment. In the future, expression of oligosaccharide modifying enzymes and secretion factors may further improve secretion rates of assembled proteins and provide heterologous proteins with altered glycoforms. Also significant is the use of BEVS as an in vivo eucaryotic laboratory to study the fundamental roles of differnt chaperones, foldases, and secretion factors. The coexpression of chaperones and foldases will complement other approaches such as the development of alternative insect cell lines, promoters, and signal peptides to optimize the baculovirus-insect cell expression system for generating high yields of valuable proteins.
BEVS 已广泛应用于重组蛋白的生产。然而，蛋白质聚集和低效加工常常限制产量，尤其是对于分泌型和膜蛋白。由于许多具有药物应用价值的蛋白质需要类似的翻译后加工步骤，因此对折叠、组装和分泌途径进行工程改造可能会提高各种有价值的复杂蛋白质的产量。应努力以低水平共表达相关伴侣蛋白或折叠酶，与最终产物协同，以确保理想的折叠和组装环境。未来，表达寡糖修饰酶和分泌因子可能进一步提高组装蛋白的分泌率，并为异源蛋白提供改变的糖型。使用 BEVS 作为体内真核实验室来研究不同伴侣蛋白、折叠酶和分泌因子的基本作用也非常重要。伴侣蛋白和折叠酶的共表达将补充其他方法，如开发替代昆虫细胞系、启动子和信号肽，以优化杆状病毒-昆虫细胞表达系统，从而产生高产量的有价值的蛋白质。
