Datema R, Romero P A, Rott R, Schwarz R T
Arch Virol. 1984;81(1-2):25-39. doi: 10.1007/BF01309294.
The alpha-glucosidase inhibitor bromoconduritol inhibits the formation of the N-linked, complex-type oligosaccharides of the glycoproteins from influenza viruses (fowl plague virus, influenza virus PR-8) and from sindbis virus. Viral glycoproteins produced in bromoconduritol-treated chicken-embryo and baby-hamster kidney cells are fully glycosylated, but accumulate N-linked, high-mannose oligosaccharides of the composition Glc1Manx (GlcNAc)2 (x = 7, 8, and 9). Other alpha-glucosidase inhibitors (nojirimycin, deoxynojirimycin, acarbose) were not specific inhibitors of oligosaccharide processing under the conditions used in the present investigation. In bromoconduritol-treated, sindbis virus-infected chicken-embryo and baby-hamster kidney cells, the sindbis glycoproteins are metabolically stable. Specific proteolytic cleavage of the polyprotein precursors to form E2 and E1 occurs in bromoconduritol-treated chicken-embryo cells, but cleavage of PE2 to E2 is prevented in the infected baby-hamster kidney cells. Yet, release of infectious sindbis virus particles is inhibited in both cell types indicating that the formation of complex oligosaccharides is required for a late step in virus formation. The release of virus particles from influenza virus PR-8-infected bromoconduritol-treated chicken-embryo cells is not inhibited, and virus with only high-mannose oligosaccharides is formed. In contrast, when chicken-embryo cells were infected with the influenza virus fowl plague virus, release of infectious particles was inhibited. The fowl plague virus hemagglutinin is cleaved in chicken-embryo cells, in contrast to the hemagglutinin of the PR-8 virus. However, the cleavage products HA1 and HA2 do not reach the cell surface. In addition, or as a consequence, HA1 and HA2 are proteolytically broken down, whereas uncleaved hemagglutinin of PR-8 appeared metabolically stable. These results may explain the decrease in formation of fowl plague virus particles and the lack of effect on PR-8 virus in bromoconduritol-treated cells. This work thus shows different biological roles for oligosaccharide processing.
α-葡萄糖苷酶抑制剂溴代康杜立醇可抑制流感病毒（禽瘟病毒、流感病毒PR - 8）和辛德毕斯病毒糖蛋白中N - 连接的复合型寡糖的形成。在经溴代康杜立醇处理的鸡胚细胞和幼仓鼠肾细胞中产生的病毒糖蛋白已完全糖基化，但会积累组成成分为Glc1Manx(GlcNAc)2（x = 7、8和9）的N - 连接的高甘露糖型寡糖。在本研究使用的条件下，其他α-葡萄糖苷酶抑制剂（诺吉霉素、脱氧野尻霉素、阿卡波糖）并非寡糖加工的特异性抑制剂。在经溴代康杜立醇处理、感染了辛德毕斯病毒的鸡胚细胞和幼仓鼠肾细胞中，辛德毕斯病毒糖蛋白在代谢上是稳定的。在经溴代康杜立醇处理的鸡胚细胞中，多蛋白前体可发生特异性蛋白水解切割以形成E2和E1，但在受感染的幼仓鼠肾细胞中，PE2向E2的切割受到抑制。然而，在这两种细胞类型中，感染性辛德毕斯病毒颗粒的释放均受到抑制，这表明复合型寡糖的形成是病毒形成后期步骤所必需的。从感染了流感病毒PR - 8且经溴代康杜立醇处理的鸡胚细胞中释放病毒颗粒未受抑制，并且形成了仅带有高甘露糖型寡糖的病毒。相比之下，当鸡胚细胞感染禽瘟病毒时，感染性颗粒的释放受到抑制。与PR - 8病毒的血凝素不同，禽瘟病毒血凝素在鸡胚细胞中会被切割。然而，切割产物HA1和HA2无法到达细胞表面。此外，或者作为结果，HA1和HA2会被蛋白水解分解，而PR - 8未切割的血凝素在代谢上似乎是稳定的。这些结果或许可以解释在经溴代康杜立醇处理的细胞中禽瘟病毒颗粒形成减少以及对PR - 8病毒无影响的原因。因此，这项工作展示了寡糖加工的不同生物学作用。
