《生命科学》 2019, 31(1): 18-26

酵母O-甘露糖转移酶的研究进展

李思强1，张敬涛2，李　慢1，李恩中1*

(1 黄淮学院生物与食品工程学院，驻马店 463000；2 枣庄市市中区食品药品监督管理局，枣庄 277100)

摘　要：摘　要：随着糖蛋白类药物的需求量不断增加，酵母表达系统的人源化改造成为当务之急。其中，酵母蛋白的O- 糖基化因O- 糖链种类繁多、组分单一以及糖基化位点预测困难等因素，限制了酵母蛋白的O- 糖基化人源化改造。从酵母蛋白的O- 糖链结构、O- 糖链发生过程及O- 糖链的功能展开综述，重点介绍起始酵母蛋白O- 糖基化过程的O- 甘露糖转移酶家族(family of protein O-mannosyltransferases， PMTs) 成员的研究现状，希望对酵母蛋白O- 糖基化人源化改造研究提供参考。

Research progress of O-mannosyltranseferases from yeast

LI Si-Qiang1， ZHANG Jing-Tao2， LI Man1， LI En-Zhong1*

(1 School of Biological and Food Engineering， Huanghuai University， Zhumadian 463000， China; 2 Shizhong District Food and Drug Administration of Zaozhuang City， Zaozhuang 277100， China)

Abstract: Abstract: With the growing global demand for glycoprotein biopharmaceuticals， the humanization of yeast expression system becomes imperative. However， the varieties of O-glycans， simple composition and unpredictable glycosylation sites have hampered the humanization of yeast O-glycosylation. This review summarized the structures， biosynthesis pathway and biological functions of O-glycans from yeast proteins and introduced O-mannosy-ltransferase family (PMTs) which catalyzed initial biosynthesis pathway of O-glycosylation， intending to provide a reference to the studies on humanization of yeast O-glycosylation.