Huismans H, van Dijk A A, Bauskin A R
Department of Biochemistry, Veterinary Research Institute, Onderstepoort, South Africa.
J Virol. 1987 Nov;61(11):3589-95. doi: 10.1128/JVI.61.11.3589-3595.1987.
A phosphorylated, nonstructural protein of bluetongue virus, NS2, is synthesized throughout the replication cycle in comparatively large amounts. The protein was detected in both the soluble and particulate fraction of the cytoplasm of infected cells. The particulate NS2 could be solubilized in 0.5 M NaCl. It was found that NS2 in the particulate fraction and immunoprecipitates of NS2 from the soluble protein fraction could be phosphorylated in vitro. It is not known whether the kinase involved is of cellular or viral origin, but after purification of NS2 by affinity chromatography on poly(U)-Sepharose it could still by phosphorylated in vitro without the addition of exogenous protein kinase. The affinity of NS2 for nucleic acid was also investigated. The protein was found to bind to single-stranded RNA. In the presence of purified bluetongue virus mRNA, NS2 formed a complex with an estimated S value of about 22S.
蓝舌病病毒的一种磷酸化非结构蛋白NS2在整个复制周期中都大量合成。该蛋白在受感染细胞细胞质的可溶性部分和颗粒部分中均被检测到。颗粒状的NS2可溶于0.5M NaCl中。研究发现，颗粒部分的NS2以及可溶性蛋白部分中NS2的免疫沉淀物在体外均可被磷酸化。尚不清楚所涉及的激酶是细胞来源还是病毒来源，但通过在聚（U）-琼脂糖凝胶上进行亲和层析纯化NS2后，在不添加外源蛋白激酶的情况下，它在体外仍可被磷酸化。还研究了NS2对核酸的亲和力。发现该蛋白可与单链RNA结合。在纯化的蓝舌病病毒mRNA存在的情况下，NS2形成了一个估计沉降系数约为22S的复合物。
