Nishimura H, Sugawara K, Gao P, Muraki Y, Hongo S, Kitame F, Nakamura K
Department of Bacteriology, Yamagata University School of Medicine, Japan.
Microbiol Immunol. 1995;39(9):737-40. doi: 10.1111/j.1348-0421.1995.tb03251.x.
The HMV-II cells infected with influenza C virus were labeled with inorganic [32P]phosphate to identify phosphorylated proteins. Analysis by radioimmunoprecipitation with antiviral serum or monoclonal antibodies revealed that three major structural proteins of the virus, hemagglutinin-esterase (HE), nucleoprotein (NP), and matrix protein (M1) are all phosphorylated in both infected cells and virions. It was also observed that, in the presence of trypsin (10 micrograms/ml), the unphosphorylated form of the HE glycoprotein was cleaved efficiently whereas the phosphorylated form was not, raising the possibility that phosphorylation of HE may influence its susceptibility to degradation by proteolytic enzymes.
用无机[32P]磷酸盐标记感染丙型流感病毒的HMV-II细胞,以鉴定磷酸化蛋白。用抗病毒血清或单克隆抗体进行放射免疫沉淀分析表明,该病毒的三种主要结构蛋白,即血凝素酯酶(HE)、核蛋白(NP)和基质蛋白(M1)在感染细胞和病毒粒子中均被磷酸化。还观察到,在胰蛋白酶(10微克/毫升)存在的情况下,HE糖蛋白的未磷酸化形式被有效切割,而磷酸化形式则未被切割,这增加了HE磷酸化可能影响其对蛋白水解酶降解敏感性的可能性。