Varicella-zoster virus p32/p36 complex is present in both the viral capsid and the nuclear matrix of the infected cell.
Varicella-zoster virus p32/p36 complex is present in both the viral capsid and the nuclear matrix of the infected cell.
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水痘-带状疱疹病毒 p32/p36 复合物存在于受感染细胞的病毒衣壳和核基质中。
DOI：
10.1128/jvi.57.1.155-164.1986
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发表时间：
1986
影响因子：
5.4
通讯作者：
Grose,C
中科院分区：
文献类型：
--
作者：
Friedrichs,WE;Grose,C
水痘带状疱疹病毒 (VZV) 指导许多糖基化和非糖基化的感染细胞特异性蛋白质的合成，其中许多蛋白质随后作为结构成分并入病毒颗粒中。在这项研究中，我们借助 VZV 特异性鼠单克隆抗体克隆 251D9 表征了非糖基化多肽复合物。通过间接免疫荧光检测，该抗体主要与位于受感染细胞核内的抗原结合，并且不附着在未受感染的细胞基质上。通过对电泳分离的感染细胞提取物进行免疫印迹分析，与 32,000 分子量的 VZV 特异性蛋白 (p32) 反应，确定单克隆抗体的多肽特异性；此外，该抗体还结合了分子量为36,000的多肽。这些抗原的合成不受糖基化抑制剂的影响。非离子或离子去污剂在溶解 p32-p36 复合物方面仅略微有效，并且高盐浓度 (2 M NaCl) 从细胞核中洗脱出相对少量的去污剂。相同的蛋白质仍然与 VZV 感染细胞的核基质相关。我们还证明该蛋白质复合物是纯化的 VZV 核衣壳的主要成分； p32 在完整衣壳和空衣壳中尤其突出。核衣壳制剂的免疫印迹分析揭示了 p32-p36 复合物中另外两个物种（p34 和 p38）。磷酸化是某些成分的显着特征。总之，这些结果表明p32-p36复合物代表了与VZV核衣壳组装和病毒DNA衣壳化密切相关的结构蛋白家族。
Varicella-zoster virus (VZV) directs the synthesis of numerous glycosylated and nonglycosylated infected-cell-specific proteins, many of which are later incorporated into the virion as structural components. In this study, we characterized a nonglycosylated polypeptide complex with the aid of a VZV-specific murine monoclonal antibody clone, 251D9. As detected by indirect immunofluorescence, the antibody bound mainly to antigens located within the nuclei of infected cells and did not attach to an uninfected cell substrate. The polypeptide specificity of the monoclonal antibody was determined by immunoblot analysis of electrophoretically separated infected cell extracts to react with a 32,000-molecular-weight VZV-specific protein (p32); in addition, the antibody also bound to a 36,000-molecular-weight polypeptide. The synthesis of these antigens was unaffected by inhibitors of glycosylation. Nonionic or ionic detergents were only marginally effective in solubilization of the p32-p36 complex, and relatively small amounts were eluted from nuclei by high salt concentrations (2 M NaCl). The same proteins remained associated with the nuclear matrix of VZV-infected cells. We also demonstrated that the protein complex was a major component of purified VZV nucleocapsids; p32 was especially prominent in both full and empty capsids. Immunoblot analysis of the nucleocapsid preparation revealed two additional species (p34 and p38) in the p32-p36 complex. Phosphorylation was a distinctive feature of some of the constituents. In summary, these results indicate that the p32-p36 complex represents a family of structural proteins closely associated with the assembly of VZV nucleocapsids and the encapsidation of viral DNA.