Lerouge P, Bardor M, Pagny S, Gomord V, Faye L
Laboratoire des Transports Intracellulaires, ESA-CNRS 6037, Université de Rouen, Faculté des Sciences, Mont Saint Aignan, France.
Curr Pharm Biotechnol. 2000 Dec;1(4):347-54. doi: 10.2174/1389201003378843.
The number of therapeutic proteins successfully produced in plants is steadily increasing and is expected to grow even more rapidly in the future. Most therapeutic proteins are glycoproteins and N-glycosylation is often essential for their stability, folding and biological activity. Recombinant glycoproteins of mammalian origin expressed in transgenic plants largely retain their biological activity. However, plants are not ideal for production of pharmaceutical proteins because they produce molecules with glycans that are not compatible with therapeutic applications in humans. As a consequence, strategies to humanise plant N-glycans are now developed. Some of these strategies involve the retention of the recombinant glycoprotein in the endoplasmic reticulum while others are related to the inhibition of endogenous Golgi glycosyltransferases or addition of "new" glycosyltransferases. Data on both the N-glycosylation of therapeutic glycoproteins produced in transgenic plants and current strategies to humanise their N-glycosylation will be discussed in this review.
在植物中成功生产的治疗性蛋白质数量正在稳步增加，预计未来增长速度会更快。大多数治疗性蛋白质是糖蛋白，N-糖基化通常对其稳定性、折叠和生物活性至关重要。在转基因植物中表达的哺乳动物来源的重组糖蛋白在很大程度上保留了它们的生物活性。然而，植物并非生产药用蛋白质的理想选择，因为它们产生的分子带有与人类治疗应用不兼容的聚糖。因此，目前正在开发使植物N-聚糖人源化的策略。其中一些策略涉及将重组糖蛋白保留在内质网中，而其他策略则与抑制内源性高尔基体糖基转移酶或添加“新的”糖基转移酶有关。本文将讨论转基因植物中生产的治疗性糖蛋白的N-糖基化数据以及当前使其N-糖基化人源化的策略。
