Milne R S, Connolly S A, Krummenacher C, Eisenberg R J, Cohen G H
Department of Microbiology, School of Dental Medicine, 215 Levy Building, 4010 Locust Street, Philadelphia, PA 19104, USA.
Virology. 2001 Mar 15;281(2):315-28. doi: 10.1006/viro.2000.0798.
Human herpesvirus entry mediator C (HveC) is an alphaherpesvirus receptor which binds to virion glycoprotein D (gD). We identified porcine HveC and studied its interaction with pseudorabies virus (PrV) and herpes simplex virus type 1 (HSV-1) gD. Porcine and human HveC have 96% amino acid identity and HveC from African green monkey, mouse, hamster, and cow are similarly conserved. Porcine HveC mediates entry of HSV-1, HSV-2, PrV, and bovine herpesvirus type 1. Truncated soluble forms of HSV-1 and PrV gD bind competitively to porcine HveC. Biosensor analysis shows that PrV gD binds with a 10-fold higher affinity than HSV-1 gD. Monoclonal antibodies against human HveC recognize the porcine homologue and can block gD binding and entry of HSV-1 and PrV. Porcine HveC is functionally indistinguishable from human HveC. Our results are consistent with the suggestion that HveC is a pan-alphaherpesvirus receptor that interacts with a conserved structural domain of gD.
人疱疹病毒进入介质C（HveC）是一种与病毒体糖蛋白D（gD）结合的α疱疹病毒受体。我们鉴定了猪HveC，并研究了其与伪狂犬病病毒（PrV）和单纯疱疹病毒1型（HSV-1）gD的相互作用。猪HveC与人HveC有96%的氨基酸同一性，来自非洲绿猴、小鼠、仓鼠和牛的HveC也有类似程度的保守性。猪HveC介导HSV-1、HSV-2、PrV和牛疱疹病毒1型的进入。HSV-1和PrV gD的截短可溶性形式竞争性结合猪HveC。生物传感器分析表明，PrV gD的结合亲和力比HSV-1 gD高10倍。抗人HveC的单克隆抗体可识别猪同源物，并能阻断HSV-1和PrV的gD结合及进入。猪HveC在功能上与人HveC没有区别。我们的结果与以下观点一致，即HveC是一种与gD保守结构域相互作用的泛α疱疹病毒受体。
