近年来,随着对空肠弯曲杆菌蛋白N-糖基化修饰系统的研究不断深入,通过关键酶PglB和外源载体蛋白的导入等,此系统在大肠杆菌中的重建成功完成。目前,已能初步利用大肠杆菌生产多种N-糖蛋白。此技术为糖蛋白疫苗的生产开辟了新的途径。此外,通过关键酶表达量的提高和糖基化位点和序列的选择等措施,大肠杆菌蛋白N-糖基化系统的糖基化效率有了进一步提高,同时改善N-糖蛋白的免疫效果的研究亦取得较大进展。这些都为大规模生产糖蛋白疫苗提供了保障。
In the last decade, the investigations into protein N-linked glycosylation system from Campylobacter jejuni become deeper and its heterologous expression in Escherichia coli through introduction of key enzyme PglB and exogenous cartier proteins continue to progress rapidly. Now several kinds of N-linked glycoprotein could be produced using this Escherichia coli recombinant system. This method provides a new and broad way for producing glycoprotein vaccines. In the meantime, such efforts as enhancement of the expression of PglB and selection of glycosylation sites as well as development in enhancing the immune efficacy of glyeoprotein have all significantly improved N-glycosylation efficiency in Escherichia coli, which lead to a good future for large- scale production of glycoprotein vaccines.