Identification of a protein kinase activity in purified foot- and-mouth disease virus
Identification of a protein kinase activity in purified foot- and-mouth disease virus
复制标题
纯化口蹄疫病毒中蛋白激酶活性的鉴定
作者：
M. Grubman;B. Baxt;J. L. La Torre;H. L. Bachrach
A型、O型和C型口蹄疫病毒的纯化制剂含有蛋白激酶活性，可以将[32P]ATP的伽马磷酸转移到病毒粒子结构蛋白VP2和VP3以及外源受体蛋白。利用硫酸鱼精蛋白作为受体，在被破坏的病毒中可以证明该激酶的活性，而在完整的病毒中则不能。该酶不耐热，最适pH为7或更高。经鉴定，硫酸鱼精蛋白中的丝氨酸残基是被蛋白激酶磷酸化的氨基酸。用裂解VP3的胰酶处理纯化的病毒，不影响蛋白激酶的活性。结果表明，口蹄疫病毒中发现的蛋白激酶活性存在于病毒或宿主来源的内部定位蛋白中。
Purified preparations of foot-and-mouth disease virus types A, O, and C contain a protein kinase activity which can transfer the gamma phosphate of [32P]ATP to virion structural proteins VP2 and VP3 and exogenous acceptor proteins. Utilizing protamine sulfate as an acceptor, the kinase activity can be demonstrated in disrupted virus but not in intact virus. The enzyme is heat labile with optimal activity at pH 7 or greater. Serine residues of protamine sulfate were identified as the amino acid phosphorylated by the protein kinase. Treatment of purified virus with trypsin, which cleaves VP3, did not affect the protein kinase activity. The results indicate that the protein kinase activity found in FMDV is present in an internally located protein of viral or host origin.