Ready K F, Sabara M I, Babiuk L A
Veterinary Infectious Disease Organization, Saskatoon, Saskatchewan, Canada.
Virology. 1988 Nov;167(1):269-73. doi: 10.1016/0042-6822(88)90077-3.
The nucleocapsid protein (VP6) and outer capsid glycoprotein (VP7) of bovine rotavirus (BRV) assemble in vitro, in 0.01 M Tris-HCl, pH 8.0, 50 mM CaCl2, into smooth particles resembling double-shelled BRV. That the two proteins interact is demonstrated by the immunoprecipitation of both by antibody directed against either VP6 or VP7. The calcium-dependence, particle morphology, and immunoreactivity in ELISA suggest that VP7 is presented authentically on the outer capsid. The implications for rotavirus morphogenesis are discussed.
牛轮状病毒（BRV）的核衣壳蛋白（VP6）和外衣壳糖蛋白（VP7）在体外于pH 8.0的0.01 M Tris-HCl、50 mM氯化钙中组装成类似双层BRV的光滑颗粒。针对VP6或VP7的抗体对两者进行免疫沉淀，证明了这两种蛋白质相互作用。ELISA中的钙依赖性、颗粒形态和免疫反应性表明VP7真实地呈现在外衣壳上。文中讨论了对轮状病毒形态发生的影响。
