Li Q, Buranathai C, Grose C, Hutt-Fletcher L M
School of Biological Sciences, University of Missouri-Kansas City, 64110, USA.
J Virol. 1997 Feb;71(2):1667-70. doi: 10.1128/JVI.71.2.1667-1670.1997.
Herpesviruses encode the complex-forming, essential glycoproteins gH and gL. Maturation and transport of gH are dependent on coexpression of its chaperone, gL. The gL proteins of alpha herpesviruses and gamma herpesviruses do not have a significant percentage of amino acid sequence homology. Yet, as we report herein, the diverse gL glycoproteins of Epstein-Barr virus (EBV) and varicella-zoster virus (VZV) were functionally interchangeable, although membrane expression and maturation of gH were separate functions for these viruses. In VZV both functions were performed by a single protein. EBV required two separate glycoproteins, one of which can be replaced by its homologous protein from VZV, a distant relative of EBV. Collectively, these results suggested that VZV gL is a simpler form of the gL chaperone protein than EBV gL.
疱疹病毒编码形成复合物的必需糖蛋白gH和gL。gH的成熟和转运依赖于其伴侣蛋白gL的共表达。α疱疹病毒和γ疱疹病毒的gL蛋白在氨基酸序列同源性上没有显著比例。然而,正如我们在此报告的,爱泼斯坦-巴尔病毒(EBV)和水痘-带状疱疹病毒(VZV)的多种gL糖蛋白在功能上是可互换的,尽管gH的膜表达和成熟对于这些病毒来说是分开的功能。在VZV中,这两种功能由单一蛋白质执行。EBV需要两种不同的糖蛋白,其中一种可以被其远亲VZV的同源蛋白取代。总体而言,这些结果表明,与EBV gL相比,VZV gL是gL伴侣蛋白的一种更简单形式。