Gerber S I, Belval B J, Herold B C
Section of Pediatric Infectious Diseases, University of Chicago, Illinois 60637-1470, USA.
Virology. 1995 Dec 1;214(1):29-39. doi: 10.1006/viro.1995.9957.
Heparan sulfate serves as a receptor for several herpesviruses. For herpes simplex virus 1 (HSV-1), pseudorabies virus, and bovine herpesvirus 1, glycoprotein C homologues have been shown to mediate the binding to cell-surface heparan sulfate. It has been assumed that glycoprotein C of HSV-2 (gC-2) plays a similar role in HSV-2 entry, but this has not been established experimentally. We first determined, using heparin-affinity chromatography, that gC-2 is a heparin-binding glycoprotein. To examine the role of gC-2 in HSV-2 infection, we constructed a gC-2 deletion mutant, HSV-2(G)gC-. In contrast to results obtained for the other alpha herpesviruses, we found that the HSV-2(G)gC- virus showed no loss in specific binding activity (particles bound/cell) or specific infectivity (PFU/particle) compared to the parental wild-type virus. Moreover, while gC-1 mutants show a marked lag in the rate of viral penetration, the gC-2-deletion virus did not. We did find that gC-2, like gC-1, protects virus from complement-mediated neutralization. These results suggest that, in contrast to HSV-1, gC-2 does not play the key role in viral binding. The major role of gC-2 may be to protect virus from complement-mediated neutralization. We speculate that serotype differences in the contribution of gC to viral binding may contribute to serotype differences in cell tropism.
硫酸乙酰肝素是几种疱疹病毒的受体。对于单纯疱疹病毒1型（HSV-1）、伪狂犬病病毒和牛疱疹病毒1型，已证明糖蛋白C同源物介导与细胞表面硫酸乙酰肝素的结合。据推测，HSV-2的糖蛋白C（gC-2）在HSV-2进入细胞过程中起类似作用，但尚未通过实验证实。我们首先使用肝素亲和色谱法确定gC-2是一种肝素结合糖蛋白。为了研究gC-2在HSV-2感染中的作用，我们构建了一个gC-2缺失突变体HSV-2(G)gC-。与其他α疱疹病毒的结果不同，我们发现与亲本野生型病毒相比，HSV-2(G)gC-病毒在特异性结合活性（结合的颗粒数/细胞）或特异性感染性（PFU/颗粒）方面没有损失。此外，虽然gC-1突变体在病毒穿透速率上有明显滞后，但gC-2缺失病毒没有。我们确实发现，与gC-1一样，gC-2可保护病毒免受补体介导的中和作用。这些结果表明，与HSV-1不同，gC-2在病毒结合中不发挥关键作用。gC-2的主要作用可能是保护病毒免受补体介导的中和作用。我们推测，gC对病毒结合贡献的血清型差异可能导致细胞嗜性的血清型差异。
