Konishi E, Mason P W
Department of Medical Zoology, Kobe University School of Medicine, Japan.
J Virol. 1993 Mar;67(3):1672-5. doi: 10.1128/JVI.67.3.1672-1675.1993.
The role of the Japanese encephalitis virus (JEV) premembrane (prM) protein in maturation of the envelope (E) glycoprotein was evaluated by using recombinant vaccinia viruses encoding E in the presence (vP829) or absence (vP658) of prM. Immunofluorescence analyses showed that E appeared to be localized in the endoplasmic reticulum of cells infected with JEV, vP829, or vP658. However, reactivity with monoclonal antibodies and behavior in Triton X-114 indicated that E produced in the absence of prM behaved abnormally. Furthermore, E produced in the presence of prM by recombinant vaccinia viruses could be incorporated into flavivirus pseudotypes, whereas E synthesized in the absence of prM could not. These results demonstrate that cosynthesis of prM is required for proper folding, membrane association, and assembly of the flavivirus E protein.
通过使用在有（vP829）或无（vP658）prM情况下编码E的重组痘苗病毒，评估了日本脑炎病毒（JEV）前膜（prM）蛋白在包膜（E）糖蛋白成熟中的作用。免疫荧光分析表明，E似乎定位于感染JEV、vP829或vP658的细胞的内质网中。然而，与单克隆抗体的反应性以及在Triton X-114中的行为表明，在没有prM的情况下产生的E表现异常。此外，重组痘苗病毒在有prM的情况下产生的E可以掺入黄病毒假型中，而在没有prM的情况下合成的E则不能。这些结果表明，prM的共合成是黄病毒E蛋白正确折叠、膜结合和组装所必需的。
