Department of Pediatrics/2501 JCP, University of Iowa Hospital, Iowa City, IA 52242, USA.
Curr Top Microbiol Immunol. 2010;342:113-28. doi: 10.1007/82_2009_4.
The VZV genome is smaller than the HSV genome and only encodes nine glycoproteins. This chapter provides an overview of three VZV glycoproteins: gH (ORF37), gL (ORF60), and gC (ORF14). All three glycoproteins are highly conserved among the alpha herpesviruses. However, VZV gC exhibits unexpected differences from its HSV counterpart gC. In particular, both VZV gC transcription and protein expression are markedly delayed in cultured cells. These delays occur regardless of the virus strain or the cell type, and may account in part for the aberrant assembly of VZV particles. In contrast to VZV gC, the general properties of gH and gL more closely resemble their HSV homologs. VZV gL behaves as a chaperone protein to facilitate the maturation of the gH protein. The mature gH protein in turn is a potent fusogen. Its fusogenic activity can be abrogated when infected cultures are treated with monoclonal anti-gH antibodies.
VZV 基因组小于 HSV 基因组，仅编码 9 种糖蛋白。本章概述了三种 VZV 糖蛋白：gH（ORF37）、gL（ORF60）和 gC（ORF14）。所有三种糖蛋白在α疱疹病毒中高度保守。然而，VZV gC 与其 HSV 对应物 gC 表现出出人意料的差异。特别是，VZV gC 的转录和蛋白表达在培养细胞中明显延迟。这些延迟与病毒株或细胞类型无关，可能部分解释了 VZV 颗粒的异常组装。与 VZV gC 不同，gH 和 gL 的一般特性更类似于它们的 HSV 同源物。VZV gL 作为一种伴侣蛋白，有助于 gH 蛋白的成熟。成熟的 gH 蛋白反过来又是一种有效的融合蛋白。当用单克隆抗 gH 抗体处理感染培养物时，其融合活性可被阻断。
