Nishikawa K, Morishima T, Toyoda T, Miyadai T, Yokochi T, Yoshida T, Nagai Y
J Virol. 1986 Dec;60(3):987-93. doi: 10.1128/JVI.60.3.987-993.1986.
Monoclonal antibodies to the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus have identified four antigenic sites on the glycoprotein, which are topologically and operationally discriminated from one another. To define the metabolisms and cellular compartments required for formation of the individual antigenic sites, a panel of monoclonal antibodies were examined for their reactivity with the nascent and variously processed forms of the antigen molecules in combination with the use of inhibitors of glycosylation (tunicamycin and N-methyl-1-deoxynojirimycin) and glycoprotein transport (carbonyl cyanide m-chlorophenylhydrazone and monensin). Reactivity was also examined with the antigen molecules deglycosylated by endoglycosidase F and with the antigen molecules reduced by 2-mercaptoethanol. The results taken together suggest that posttranslational organization of the glycoprotein is important for all four of the antigenic sites. At the same time, there appeared to be marked site-specific requirements with respect to glycosylation and disulfide bond formation. However, all of these metabolic requirements were found to be provided within the rough endoplasmic reticulum, and no further processing of the antigen molecules appeared to be necessary for the formation of any of the antigenic sites.
针对新城疫病毒血凝素 - 神经氨酸酶糖蛋白的单克隆抗体已鉴定出该糖蛋白上的四个抗原位点，这些位点在拓扑结构和功能上相互区分。为了确定形成各个抗原位点所需的代谢过程和细胞区室，结合使用糖基化抑制剂（衣霉素和N - 甲基 - 1 - 脱氧野尻霉素）和糖蛋白转运抑制剂（羰基氰化物间氯苯腙和莫能菌素），检测了一组单克隆抗体与抗原分子的新生形式及各种加工形式的反应性。还检测了用内切糖苷酶F去糖基化的抗原分子以及用2 - 巯基乙醇还原的抗原分子的反应性。综合结果表明，糖蛋白的翻译后组装对所有四个抗原位点都很重要。同时，在糖基化和二硫键形成方面似乎存在明显的位点特异性要求。然而，所有这些代谢需求都在粗面内质网内得到满足，并且抗原分子似乎无需进一步加工即可形成任何抗原位点。
