Namazue J, Campo-Vera H, Kitamura K, Okuno T, Yamanishi K
Virology. 1985 May;143(1):252-9. doi: 10.1016/0042-6822(85)90112-6.
Monoclonal antibodies to varicella zoster virus (VZV) glycoproteins were used to study the processing of three glycoproteins with molecular weights of 83K-94K (gp 2), 64K (gp 3), and 55K (gp 5). Immunoprecipitation experiments performed with VZV-infected cells, pulse labeled with [3H]glucosamine in the presence of tunicamycin, suggest that O-linked oligosaccharide is present on the glycoprotein of gp 2. Use of the enzyme endo-beta-N-acetylglucosaminidase H revealed that the fully processed form of gp 3 had high-mannose type and that of gp 5 had only complex type of N-linked oligosaccharides. Experiments with monensin suggest that the precursor form (116K) of gp 3 is cleaved during the processing from Golgi apparatus to cell surface membrane. The extension of O-linked oligosaccharide chain and the complex type of N-linked oligosaccharide chains also occurs during this processing.
水痘带状疱疹病毒（VZV）糖蛋白单克隆抗体被用于研究三种分子量分别为83K - 94K（gp 2）、64K（gp 3）和55K（gp 5）的糖蛋白的加工过程。在用衣霉素存在的情况下用[3H]葡糖胺脉冲标记的VZV感染细胞进行的免疫沉淀实验表明，O-连接寡糖存在于gp 2的糖蛋白上。使用内切β-N-乙酰葡糖胺糖苷酶H显示，gp 3的完全加工形式具有高甘露糖型，而gp 5的完全加工形式仅具有复杂型的N-连接寡糖。莫能菌素实验表明，gp 3的前体形式（116K）在从高尔基体到细胞表面膜的加工过程中被切割。O-连接寡糖链和复杂型N-连接寡糖链的延伸也发生在这个加工过程中。
