Lab of Cellular Oncology, Center for Cancer Research, NCI, USA.
Virology. 2013 Oct;445(1-2):169-74. doi: 10.1016/j.virol.2013.05.038. Epub 2013 Jun 22.
The elegant icosahedral surface of the papillomavirus virion is formed by a single protein called L1. Recombinant L1 proteins can spontaneously self-assemble into a highly immunogenic structure that closely mimics the natural surface of native papillomavirus virions. This has served as the basis for two highly successful vaccines against cancer-causing human papillomaviruses (HPVs). During the viral life cycle, the capsid must undergo a variety of conformational changes, allowing key functions including the encapsidation of the ~8 kb viral genomic DNA, maturation into a more stable state to survive transit between hosts, mediating attachment to new host cells, and finally releasing the viral DNA into the newly infected host cell. This brief review focuses on conserved sequence and structural features that underlie the functions of this remarkable protein.
乳头瘤病毒病毒粒子的优雅的二十面体表面由一种称为 L1 的单一蛋白质形成。重组 L1 蛋白可以自发地自我组装成一种高度免疫原性的结构,该结构与天然乳头瘤病毒病毒粒子的自然表面非常相似。这是针对致癌型人乳头瘤病毒 (HPV) 的两种非常成功的疫苗的基础。在病毒生命周期中,衣壳必须经历多种构象变化,从而允许包括以下关键功能:将约 8kb 的病毒基因组 DNA 包裹在内、成熟为更稳定的状态以在宿主之间的运输过程中存活、介导与新宿主细胞的附着,以及最终将病毒 DNA释放到新感染的宿主细胞中。本综述重点介绍了构成这种出色蛋白质功能基础的保守序列和结构特征。