MATURATION OF JAPANESE ENCEPHALITIS-VIRUS GLYCOPROTEINS PRODUCED BY INFECTED MAMMALIAN AND MOSQUITO CELLS
MATURATION OF JAPANESE ENCEPHALITIS-VIRUS GLYCOPROTEINS PRODUCED BY INFECTED MAMMALIAN AND MOSQUITO CELLS
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DOI：
10.1016/0042-6822(89)90161-x
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发表时间：
1989-04-01
期刊：
影响因子：
3.7
通讯作者：
MASON, PW
中科院分区：
文献类型：
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作者：
MASON, PW
乙脑感染脊椎动物和无脊椎动物细胞系对乙脑病毒结构糖蛋白(E)和两种非结构糖蛋白(NS1和NS1‘’)进行了不同的处理。感染乙脑的猴细胞(Vero细胞)缓慢释放三种蛋白质(T1/2和GT；6小时)。蚊虫细胞株以相似的速率释放E(T1/2和8小时)，而NS1和NS1‘’以未降解的形式保留在细胞层中。在两种细胞类型中，这三种蛋白质的蛋白质降解过程似乎是相同的，但在N-连接糖基化方面观察到了一些差异。在两种类型的感染细胞中发现的E、NS1和NS1‘’在合成后8小时以上都含有高甘露糖寡糖基。单独的E蛋白寡糖组在从Vero细胞释放之前添加额外的糖残留物，而E蛋白寡糖组在从蚊子细胞释放之前削减糖残留物。在感染的Vero细胞培养液中发现的NS1和NS1‘’形式含有一个复合体和一个高甘露低聚糖。乙脑感染的Vero细胞所释放的三种糖蛋白均与胞外颗粒有关，E株为病毒颗粒，NS1和NS1‘’株为低密度颗粒。此外，在Triton X-114提取实验中，E、NS1和NS1‘’表现出两亲性。综上所述，这些结果表明，结构性(E)和非结构性(NS1和NS1‘’)糖蛋白都积聚在感染的Vero细胞的分泌途径中，组装成颗粒，然后释放到细胞外液中。
The Japanese encephalitis virus (JE) structural glycoprotein (E) and two nonstructural glycoproteins (NS1 and NS1'') were processed differently by JE-infected vertebrate and invertebrate cell lines. All three proteins were released slowly (t1/2 > 6 hr) from JE-infected monkey cells (Vero cells). Mosquito cell lines released E at a similar rate (t1/2 > 8 hr), while NS1 and NS1'' were retained in an undegraded form in the cell layer. The proteolytic processing of the three proteins appeared identical in both cell types, but some differences in N-linked glycosylation were observed. E, NS1, and NS1'' found within the infected cells of both types contained high-mannose oligosaccharide groups for more than 8 hr after synthesis. Additional sugar residues were added to the single E protein oligosaccharide group prior to release from Vero cells, while sugar residues were trimmed from the E protein oligosaccharide group prior to release from mosquito cells. The forms of NS1 and NS1'' found in the culture fluid of infected Vero cells contained one complex and one high-mannose oligosaccharide. All three glycoproteins released from JE-infected Vero cells were associated with extracellular particles, the virion in the case of E and a low density particle in the case of NS1 and NS1''. Furthermore, E, NS1, and NS1'' exhibited amphipathic properties in Triton X-114 extraction experiments. Taken together, these results suggest that both the structural (E) and nonstructural (NS1 and NS1'') glycoproteins were accumulated within the secretory pathway of the infected Vero cells, assembled into particles, and then released into the extracellular fluid.