昆虫杆状病毒系统表达外源蛋白的糖基化  

The Progress in Glycosylation of Recombinant Protein Expressed by Baculovirus-insect System

作　　者：陈璟[1] 方宏清[1] 周长林[2] 陈惠鹏[1] 

机构地区：[1]军事医学科学院生物工程研究所,北京100071 [2]中国药科大学,南京210009

出　　处：《中国生物工程杂志》2004年第3期1-6,共6页China Biotechnology

摘　　要：昆虫表达系统作为一类应用广泛的真核表达系统 ,具有与多数高等真核生物相类似的翻译后修饰的过程。但其生产的重组糖蛋白一般仅具有高甘露糖或寡甘露糖型糖链 ,难以生成复杂构型糖链成为该系统的缺陷之一。综述了目前昆虫杆状病毒系统表达外源蛋白的糖基化研究进展。As a widely used eukaryotic expression system,baculovirus\|insect expression vector system(BEVS) has the same process of post\|translation modification as most higher eukaryotic expression system.But the recombinant glycoproteins produced by BEVS usually have paucimannose or highmannose glycan,while mammalian glycosylation usually have complex glcans which maybe essential to function.The lack of complex glycosylation has limited the use of BEVS despite its high productivity and versatility.Researchers try to reconstruct some new cell lines or baculovirus vectors which have the gene of mammalian glycosylation process enzymes,using these variety of strategies could improve the complexity of the glycosylation produced by BEVS.And the progress in glycosylation of recombinant protein expressed by baculovirus insect system was reviewed.

关 键 词：昆虫 表达系统 杆状病毒 糖基化 翻译 修饰 

分 类 号：Q78[生物学—分子生物学] Q753