Patzer E J, Nakamura G R, Yaffe A
J Virol. 1984 Aug;51(2):346-53. doi: 10.1128/JVI.51.2.346-353.1984.
The oligosaccharide processing and secretion of hepatitis B surface antigen (HBsAg) was studied in Chinese hamster ovary cells stably transfected with the gene coding HBsAg. HBsAg was secreted from cells with a relatively long half time (ca. 5 h). This appeared to be a characteristic of HBsAg itself, since HBsAg-producing cells infected with vesicular stomatitis virus transported the viral envelope glycoprotein to the cell surface with normal kinetics (half time of ca. 30 min). The secreted HBsAg was comprised of both the unglycosylated (P20) and the glycosylated (G25) polypeptides, characteristic of HBsAg isolated from human serum or secreted from other cell lines (C. W. Crowley, C.-C. Liu, and A. D. Levinson, Mol. Cell. Biol. 3:44-55, 1983; M. F. Dubois, C. Pourcel, S. Rousset, C. Chang, and P. Tiollais, Proc. Natl. Acad. Sci. U.S.A. 77:4549-4553, 1980; C.-C. Liu, D. Yansura, and A. D. Levinson, DNA, 1:213-221, 1982; G. M. Macnab, J. J. Alexander, G. Lecatsas, E. M. Bey, and J. M. Urbanocvicz, Br. J. Cancer, 24:509-515, 1976; A. M. Moriarity, B. H. Hoyer, J. W.-K. Shih, J. L. Gerin, and D. H. Hamer, Proc. Natl. Acad. Sci. U.S.A. 78:2606-2610, 1981; D. L. Peterson, J. Biol. Chem., 256:6975-6983, 1981). The glycosylated polypeptide (GP25) contained complex oligosaccharide chains. Cell-associated HBsAg also was comprised of both an unglycosylated and a glycosylated polypeptide; however, the glycosylated form (GP23) contained only high-mannose oligosaccharide chains. No oligosaccharide processing of the high-mannose chains could be detected within the cells. Thus, most of the time before secretion of HBsAg from cells must have been spent in a pre-Golgi or early Golgi compartment. Glycosylation was inhibited completely by tunicamycin, although unglycosylated particles were still secreted from cells and were antigenic. The secretion and oligosaccharide processing of HBsAg were inhibited with high concentrations of monensin, but at lower concentrations of monensin HBsAg was still secreted, although only half of the oligosaccharide chains were processed to the complex form.
在稳定转染了编码乙肝表面抗原（HBsAg）基因的中国仓鼠卵巢细胞中，对HBsAg的寡糖加工和分泌进行了研究。HBsAg从细胞中分泌出来的半衰期相对较长（约5小时）。这似乎是HBsAg自身的一个特性，因为感染水疱性口炎病毒的产生HBsAg的细胞将病毒包膜糖蛋白以正常动力学（半衰期约30分钟）转运到细胞表面。分泌的HBsAg由未糖基化的（P20）和糖基化的（G25）多肽组成，这是从人血清中分离或从其他细胞系分泌的HBsAg的特征（C.W.克劳利、C.-C.刘和A.D.莱文森，《分子细胞生物学》3:44 - 55，1983；M.F.杜布瓦、C.普尔塞尔、S.鲁塞、C.张和P.蒂奥利斯，《美国国家科学院院刊》77:4549 - 4553，1980；C.-C.刘、D.扬苏拉和A.D.莱文森，《DNA》，1:213 - 221，1982；G.M.麦克纳布、J.J.亚历山大、G.莱卡萨、E.M.贝伊和J.M.乌尔巴诺维茨，《英国癌症杂志》，24:509 - 5,15，1976；A.M.莫里亚蒂、B.H.霍耶、J.W.-K.施、J.L.格林和D.H.哈默，《美国国家科学院院刊》78:2606 - 2610，1981；D.L.彼得森，《生物化学杂志》，256:6975 - 6983，1981）。糖基化多肽（GP25）含有复杂的寡糖链。细胞相关的HBsAg也由未糖基化和糖基化的多肽组成；然而，糖基化形式（GP23）仅含有高甘露糖寡糖链。在细胞内未检测到高甘露糖链的寡糖加工。因此，HBsAg从细胞分泌之前的大部分时间必定是在高尔基体前体或早期高尔基体区室中度过的。衣霉素完全抑制了糖基化，尽管未糖基化的颗粒仍从细胞中分泌出来且具有抗原性。高浓度的莫能菌素抑制了HBsAg的分泌和寡糖加工，但在较低浓度的莫能菌素下，HBsAg仍能分泌，尽管只有一半的寡糖链被加工成复杂形式。
