Hollister J R, Jarvis D L
Department of Molecular Biology, University of Wyoming, P.O. Box 3944, Laramie, WY 82071-3944, USA.
Glycobiology. 2001 Jan;11(1):1-9. doi: 10.1093/glycob/11.1.1.
Recombinant mammalian glycoproteins produced by the baculovirus-insect cell expression system usually do not have structurally authentic glycans. One reason for this limitation is the virtual absence in insect cells of certain glycosyltransferases, which are required for the biosynthesis of complex, terminally sialylated glycoproteins by mammalian cells. In this study, we genetically transformed insect cells with mammalian beta 1,4-galactosyltransferase and alpha 2,6-sialyltransferase genes. This produced a new insect cell line that can express both genes, serve as hosts for baculovirus infection, and produce foreign glycoproteins with terminally sialylated N-glycans.
杆状病毒-昆虫细胞表达系统产生的重组哺乳动物糖蛋白通常不具有结构上真实的聚糖。造成这种局限性的一个原因是昆虫细胞中几乎不存在某些糖基转移酶，而这些酶是哺乳动物细胞生物合成复杂的、末端唾液酸化糖蛋白所必需的。在本研究中，我们用哺乳动物β1,4-半乳糖基转移酶和α2,6-唾液酸转移酶基因对昆虫细胞进行了基因转化。这产生了一种新的昆虫细胞系，它可以表达这两种基因，作为杆状病毒感染的宿主，并产生具有末端唾液酸化N-聚糖的外源糖蛋白。
