Matsumura H, Futaesaku Y, Kohno S, Sugiura A, Kohase M
Department of Measles Virus, National Institute of Health, Tokyo, Japan.
J Virol. 1990 Mar;64(3):1410-3. doi: 10.1128/JVI.64.3.1410-1413.1990.
A temperature-sensitive mutant (ts3) of Newcastle disease virus was physiologically characterized. All major viral structural proteins were synthesized at the permissive (37 degrees C) and nonpermissive (42 degrees C) temperatures, but the fusion (F) glycoprotein was not cleaved at 42 degrees C. In immunocytochemical electron microscopy, the F protein was abundant in the rough endoplasmic reticulum but not in cytoplasmic membrane at 42 degrees C. Noninfectious hemagglutinating virus particles containing all major structural proteins except the F protein were released at 42 degrees C from infected cells. We concluded that the defect in ts3 resides in the intracellular processing of the F protein.
对新城疫病毒的一个温度敏感突变体（ts3）进行了生理学特性分析。在允许温度（37摄氏度）和非允许温度（42摄氏度）下均能合成所有主要病毒结构蛋白，但融合（F）糖蛋白在42摄氏度时未被切割。在免疫细胞化学电子显微镜下，42摄氏度时F蛋白在内质网中大量存在，但在细胞质膜中不存在。在42摄氏度时，含有除F蛋白外所有主要结构蛋白的非感染性血凝病毒颗粒从感染细胞中释放出来。我们得出结论，ts3的缺陷在于F蛋白的细胞内加工过程。
