Le Blois H, French T, Mertens P P, Burroughs J N, Roy P
Department of Molecular Biophysics, University of Oxford, United Kingdom.
Virology. 1992 Aug;189(2):757-61. doi: 10.1016/0042-6822(92)90600-t.
A minor core protein, VP4, of bluetongue virus serotype 10 (BTV-10) has been synthesized in insect cells infected with a genetically manipulated recombinant baculovirus. When insect cells were coinfected by this recombinant virus and a recombinant baculovirus expressing the two major core proteins (VP3 and VP7) of the virus, core-like particles (CLPs) consisting of all three proteins were formed. Purified CLPs reacted with [32P]GTP which was covalently bound to VP4 only. Similarly reconstituted CLPs with VP1 or VP6 did not form covalent complexes with [32P]GTP. The virion-derived VP4 was also shown to have GTP-binding activity. The covalent binding of GTP indicates that expressed VP4 not only is biologically active but also is the candidate guanylyl transferase of the virus. The optimum reaction conditions for GTP binding by VP4 have been investigated.
蓝舌病病毒10型（BTV-10）的一种次要核心蛋白VP4已在感染了基因工程重组杆状病毒的昆虫细胞中合成。当昆虫细胞被这种重组病毒与一种表达该病毒两种主要核心蛋白（VP3和VP7）的重组杆状病毒共感染时，由这三种蛋白组成的类核心颗粒（CLP）形成。纯化的CLP与仅共价结合到VP4上的[32P]GTP发生反应。同样，用VP1或VP6重构的CLP不与[32P]GTP形成共价复合物。病毒衍生的VP4也显示具有GTP结合活性。GTP的共价结合表明表达的VP4不仅具有生物活性，而且是该病毒的候选鸟苷酸转移酶。已经研究了VP4结合GTP的最佳反应条件。
