Brookman J L, Stott A J, Cheeseman P J, Burns N R, Adams S E, Kingsman A J, Gull K
School of Biological Sciences, University of Manchester, United Kingdom.
Virology. 1995 Feb 20;207(1):59-67. doi: 10.1006/viro.1995.1051.
We present an immunological characterization of the Ty1 virus-like particle (VLP). A panel of monoclonal and polyclonal antibodies were raised against the TYA particle-forming protein. Using these antibodies in epitope availability assays two N-terminal regions of the TYA protein were mapped projecting from or at the surface of the proteinaceous shell of the VLP. Two different C-termini of the TYA protein, corresponding to the C-terminus of the full-length and truncated forms, were seen to be buried within the particle core and not available for antibody binding. RNase accessibility studies demonstrated a difference in the porosity of the protein shell surrounding the Ty1 nucleic acid between different particle types, suggesting differences in subunit organization.
我们展示了Ty1病毒样颗粒（VLP）的免疫学特征。制备了一组针对TYA颗粒形成蛋白的单克隆和多克隆抗体。在表位可及性分析中使用这些抗体，绘制出TYA蛋白的两个N端区域，它们从VLP蛋白质外壳表面突出或位于其表面。TYA蛋白的两个不同C端，分别对应全长和截短形式的C端，被发现埋在颗粒核心内，无法与抗体结合。核糖核酸酶可及性研究表明，不同颗粒类型之间围绕Ty1核酸的蛋白质外壳孔隙率存在差异，这表明亚基组织存在差异。
