许多哺乳动物的疱疹病毒利用一半作为受体在房间表面 proteoglycans 上介绍的 heparan 硫酸盐(HS ) 因为房间入口,和这个过程也要求病毒的 glycoprotein C (gC ) 相当或相同事物。然而,我们在便于象鸭瘟疫病毒(DPV ) 那样的另外的 alpha 疱疹病毒的附件的 gC 的角色的理解仍然保持初步。在 DPV 感染期间学习 gC 的角色,我们使用了一个删除 gC 的变异的病毒(DPV-gC-EGFP ) 。由即时 PCR 的病毒的拷贝数字的检查,以及病毒的吸附和增长的时间功课研究表明 gC 涉及病毒的绑定到房间表面。到 HS 的病毒的 glycoproteins (gB-DPV, gC-DPV,和 gE-DPV ) 的亲密关系用一个原核生物的表示系统和 HiTrap 肝磷脂 HP 列层析被估计。另外,在在 DPV 和 HS 之间的相互作用起了一个作用证实那 gC,病毒与 HS 类似物肝磷脂被对待,宿主细胞在暴露以前与它的禁止者 heparinase 被对待到 DPV-gC-EGFP 或野类型的紧张汉语剧毒的鸭瘟疫病毒(DPV-CHv ) 。病毒传染性上的肝磷脂和 heparinase 的效果证明病毒的吸附上的 gC 的那功能在房间表面上独立于在 gC 和肝磷脂硫酸盐之间的相互作用。总的来说,这研究证明 DPV 的 gC 能调停以一种 HS 独立的方式的病毒的吸附,它把它与一些另外的 alpha 疱疹病毒的 gC 区分开来。未来研究将被要求识别涉及 gC 蛋白质绑定到房间的受体。这个工作提供我们为在鸭瘟疫病毒感染期间在吸附检验 gC 的角色的进一步的研究的一个基础。
Many mammalian herpes viruses utilize heparan sulfate (HS) moieties present on cell surface proteoglycans as receptors for cell entry, and this process also requires viral glycoprotein C (gC) homologues. However, our understanding of the role of gC in facilitating attachment of other alpha-herpes viruses such as the duck plague virus (DPV) remains preliminary. To study the role of gC during DPV infection, we used a gC-deleted mutant virus (DPV-AgC-EGFP). Examination of the viral copy number by real-time PCR, as well as time course studies of viral adsorption and proliferation revealed that gC was involved in the viral binding to the cell surface. The affinity of viral glycoproteins (gB-DPV, gC-DPV, and gE-DPV) to HS was assessed using a prokaryotic expression system and HJTrapTM HeparJn HP column chromatography. In addition, to confirm that gC played a role in the interaction between DPV and HS, viruses were treated with the HS analogue heparin and host cells were treated with its inhibitors heparinase prior to exposure to DPV-△gC-EGFP or wild-type strain Chinese virulent duck plague virus (DPV-CHv). The effects of heparin and heparinase on virus infectivity demonstrated that function of gC on Viral adsorption is independent of interactions between gC and heparin sulfate on cell surface. All in all, this study demonstrated that the gC of DPV can mediate viral adsorption in an HS-independent manner, which distinguish it from the gC of some other alpha-herpes viruses. Future studies will be required to identify the receptors involved in gC protein binding to cells. This work provides us a foundation for further studies of examining the roles of gC in the adsorption during duck plague virus infection.