Takeuchi K, Tanabayashi K, Hishiyama M, Yamada A
Department of Viral Disease and Vaccine Control, National Institute of Health, Tokyo, Japan.
Virology. 1996 Nov 1;225(1):156-62. doi: 10.1006/viro.1996.0583.
By immunoprecipitation analysis using antisera against oligo peptides synthesized based on the deduced N-terminal and C-terminal amino acid sequences of the SH proteins of the mumps virus, the SH protein was detected in mumps virus-infected cells. The SH protein expressed from cDNA by the vaccinia-T7 expression system was recovered in the membrane fraction. Association of the SH protein with the membrane was resistant to high salt, EDTA, and alkaline treatment but sensitive to detergents. Indirect immunofluorescence experiments showed that the SH protein is involved in the exocytotic pathway. These data indicate that the SH protein is a membrane protein. Treatment of microsomes with TPCK-trypsin suggested that the SH protein is oriented in the membrane with its C-terminal facing the cytoplasm. Furthermore the SH protein was not detected in a particular strain (Enders strain) of mumps virus, indicating that the mumps virus SH protein is not essential for virus replication.
通过使用针对基于腮腺炎病毒SH蛋白推导的N端和C端氨基酸序列合成的寡肽的抗血清进行免疫沉淀分析，在腮腺炎病毒感染的细胞中检测到了SH蛋白。通过痘苗-T7表达系统从cDNA表达的SH蛋白在膜组分中被回收。SH蛋白与膜的结合对高盐、EDTA和碱性处理具有抗性，但对去污剂敏感。间接免疫荧光实验表明，SH蛋白参与胞吐途径。这些数据表明SH蛋白是一种膜蛋白。用TPCK-胰蛋白酶处理微粒体表明，SH蛋白在膜中的取向是其C端面向细胞质。此外，在腮腺炎病毒的一个特定毒株（恩德斯毒株）中未检测到SH蛋白，这表明腮腺炎病毒SH蛋白对于病毒复制不是必需的。
