Heming Jason D, Conway James F, Homa Fred L
Department of Biological Sciences, Duquesne University, Pittsburgh, PA, 15282, USA.
Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, 15261, USA.
Adv Anat Embryol Cell Biol. 2017;223:119-142. doi: 10.1007/978-3-319-53168-7_6.
Herpes simplex virus type I (HSV-1) is the causative agent of several pathologies ranging in severity from the common cold sore to life-threatening encephalitic infection. During productive lytic infection, over 80 viral proteins are expressed in a highly regulated manner, resulting in the replication of viral genomes and assembly of progeny virions. The virion of all herpesviruses consists of an external membrane envelope, a proteinaceous layer called the tegument, and an icosahedral capsid containing the double-stranded linear DNA genome. The capsid shell of HSV-1 is built from four structural proteins: a major capsid protein, VP5, which forms the capsomers (hexons and pentons), the triplex consisting of VP19C and VP23 found between the capsomers, and VP26 which binds to VP5 on hexons but not pentons. In addition, the dodecameric pUL6 portal complex occupies 1 of the 12 capsid vertices, and the capsid vertex specific component (CVSC), a heterotrimer complex of pUL17, pUL25, and pUL36, binds specifically to the triplexes adjacent to each penton. The capsid is assembled in the nucleus where the viral genome is packaged into newly assembled closed capsid shells. Cleavage and packaging of replicated, concatemeric viral DNA requires the seven viral proteins encoded by the UL6, UL15, UL17, UL25, UL28, UL32, and UL33 genes. Considerable advances have been made in understanding the structure of the herpesvirus capsid and the function of several of the DNA packaging proteins by applying biochemical, genetic, and structural techniques. This review is a summary of recent advances with respect to the structure of the HSV-1 virion capsid and what is known about the function of the seven packaging proteins and their interactions with each other and with the capsid shell.
I型单纯疱疹病毒（HSV-1）是多种疾病的病原体，其严重程度从常见的唇疱疹到危及生命的脑炎感染不等。在 productive 溶细胞感染期间，超过80种病毒蛋白以高度调控的方式表达，导致病毒基因组的复制和子代病毒粒子的组装。所有疱疹病毒的病毒粒子都由一个外部膜包膜、一层称为皮层的蛋白质层和一个包含双链线性DNA基因组的二十面体衣壳组成。HSV-1的衣壳壳由四种结构蛋白构成：一种主要衣壳蛋白VP5，它形成衣壳粒（六邻体和五邻体）；位于衣壳粒之间的由VP19C和VP23组成的三聚体；以及与六邻体上的VP5结合但不与五邻体结合的VP26。此外，十二聚体pUL6门户复合体占据12个衣壳顶点中的1个，衣壳顶点特异性成分（CVSC）是一种由pUL17、pUL25和pUL36组成的异源三聚体复合体，它特异性地结合到每个五邻体相邻的三聚体上。衣壳在细胞核中组装，病毒基因组被包装到新组装的封闭衣壳壳中。复制的串联病毒DNA的切割和包装需要由UL6、UL15、UL17、UL25、UL28、UL32和UL33基因编码的七种病毒蛋白。通过应用生化、遗传和结构技术，在理解疱疹病毒衣壳的结构以及几种DNA包装蛋白的功能方面取得了相当大的进展。本综述总结了关于HSV-1病毒粒子衣壳结构以及七种包装蛋白的功能、它们彼此之间以及与衣壳壳的相互作用的最新进展。 （注：原文中“productive”可能有误，推测可能是“productive”，可根据实际情况调整译文）
