Söderlund H, von Bonsdorff C H, Ulmanen I
J Gen Virol. 1979 Oct;45(1):15-26. doi: 10.1099/0022-1317-45-1-15.
The envelope spikes of Sindbis and Semliki Forest virus are arranged in a T = 4 icosahedral surface lattice and, by deduction, it has been suggested that the nucleocapsid proteins are similarly arranged. After treatment of the virions with a non-ionic detergent the released nucleocapsids sediment in sucrose gradients at about 160S and 150S and have densities in CsCl of 1.42 g/ml and 1.425 g/ml, respectively, for Sindbis and Semliki Forest virus. At pH 6.0 Sindbis nucleocapsids do not contract like those of Semliki Forest virus. Nucleocapsids of both viruses are sensitive to the action of ribonuclease but only those of Semliki Forest virus undergo a drastic structural rearrangement due to the treatment. EDTA treatment in hypotonic conditions results in a decrease in the S-value for both particles. Electron micrographs show that the SFV nucleocapsids are partly 'unfolded' while those of Sindbis appear slightly contracted after exposure to EDTA.
辛德毕斯病毒和塞姆利基森林病毒的包膜刺突排列成T = 4二十面体表面晶格,由此推断,有人认为核衣壳蛋白也有类似的排列方式。用非离子去污剂处理病毒粒子后,释放出的核衣壳在蔗糖梯度中以约160S和150S沉降,对于辛德毕斯病毒和塞姆利基森林病毒,其在氯化铯中的密度分别为1.42 g/ml和1.425 g/ml。在pH 6.0时,辛德毕斯病毒的核衣壳不像塞姆利基森林病毒的核衣壳那样收缩。两种病毒的核衣壳都对核糖核酸酶的作用敏感,但只有塞姆利基森林病毒的核衣壳因这种处理而发生剧烈的结构重排。在低渗条件下用乙二胺四乙酸(EDTA)处理会导致两种粒子的S值降低。电子显微镜照片显示,塞姆利基森林病毒的核衣壳部分“展开”,而辛德毕斯病毒的核衣壳在暴露于EDTA后似乎略有收缩。