van Drunen Littel-van den Hurk S, Babiuk L A
Virology. 1985 May;143(1):104-18. doi: 10.1016/0042-6822(85)90100-x.
The effect of tunicamycin and monensin on the biosynthesis, intracellular transport, and maturation of bovine herpesvirus type-1 (BHV-1) glycoproteins was examined. Tunicamycin completely inhibited the production of infectious virus particles and significantly reduced the incorporation of [3H]glucosamine into viral glycoproteins. In the presence of monensin, reduced amounts of infectious virus particles were produced, which was mainly due to inhibition of virus release, rather than virus production. Monensin only slightly inhibited viral glycoprotein synthesis. The effects of these compounds on infectivity indicated that glycosylation is required for the production of infectious virus, though complete processing of the glycoproteins is not essential. In addition, egress of the virions from infected cells probably requires a functional Golgi complex. In the presence of tunicamycin or monensin various degrees of glycosylation of the major glycoproteins occurred, consequently their rates of migration differed from that of the normal glycoproteins. Tunicamycin completely blocked glycosylation of GVP 6/11a/16 and GVP 7. In contrast, GVP 3/9 and GVP 11b were partially glycosylated in the presence of tunicamycin. These results indicated that GVP 6/11a/16 and GVP 7 are N-linked glycoproteins, but GVP 3/9 and GVP 11b contain both N- and O-linked oligosaccharide side chains. Tunicamycin blocked the transport of all viral glycoproteins to the cell surface, suggesting that glycosylation is required for this process. In the presence of monensin, the viral glycoproteins were transported and expressed on the cell surface indicating that transport does not require complete processing of the glycoproteins and may occur via a Golgi-independent pathway. In addition, monensin-treated BHV-1 infected cells could act as target cells in an antibody-dependent cell cytotoxicity assay. Thus, complete glycosylation may not be essential for maintenance of antigenicity and participation in immune destruction.
研究了衣霉素和莫能菌素对牛疱疹病毒1型（BHV-1）糖蛋白生物合成、细胞内运输及成熟的影响。衣霉素完全抑制感染性病毒颗粒的产生，并显著降低[3H]葡糖胺掺入病毒糖蛋白的量。在莫能菌素存在的情况下，产生的感染性病毒颗粒数量减少，这主要是由于病毒释放受到抑制，而非病毒产生受到抑制。莫能菌素仅轻微抑制病毒糖蛋白的合成。这些化合物对感染性的影响表明，糖基化是产生感染性病毒所必需的，尽管糖蛋白的完全加工并非必不可少。此外，病毒粒子从感染细胞中释放可能需要一个功能正常的高尔基体复合体。在衣霉素或莫能菌素存在的情况下，主要糖蛋白发生了不同程度的糖基化，因此它们的迁移速率与正常糖蛋白不同。衣霉素完全阻断了GVP 6/11a/16和GVP 7的糖基化。相比之下，在衣霉素存在的情况下，GVP 3/9和GVP 11b发生了部分糖基化。这些结果表明，GVP 6/11a/16和GVP 7是N-连接糖蛋白，但GVP 3/9和GVP 11b同时含有N-连接和O-连接的寡糖侧链。衣霉素阻断了所有病毒糖蛋白向细胞表面的运输，表明糖基化是这一过程所必需的。在莫能菌素存在的情况下，病毒糖蛋白被运输并表达在细胞表面，这表明运输不需要糖蛋白的完全加工，可能通过一条不依赖高尔基体的途径发生。此外，经莫能菌素处理的BHV-1感染细胞在抗体依赖性细胞毒性试验中可作为靶细胞。因此，完全糖基化对于维持抗原性和参与免疫破坏可能并非必不可少。
