Dubin G, Socolof E, Frank I, Friedman H M
Department of Medicine, University of Pennsylvania, Philadelphia.
J Virol. 1991 Dec;65(12):7046-50. doi: 10.1128/JVI.65.12.7046-7050.1991.
Recent studies indicate that the herpes simplex virus type 1 (HSV-1) Fc receptor (FcR) can bind antiviral immunoglobulin G by participating in antibody bipolar bridging. This occurs when the Fab domain of an immunoglobulin G molecule binds to its antigenic target and the Fc domain binds to the HSV-1 FcR. In experiments comparing cells infected with wild-type HSV-1 (NS) and cells infected with an FcR-deficient mutant (ENS), we demonstrate that participation of the HSV-1 FcR in antibody bipolar bridging reduces the effectiveness of antibody-dependent cellular cytotoxicity.
最近的研究表明,1型单纯疱疹病毒(HSV-1)Fc受体(FcR)可通过参与抗体双极桥接来结合抗病毒免疫球蛋白G。当免疫球蛋白G分子的Fab结构域与其抗原靶标结合且Fc结构域与HSV-1 FcR结合时,就会发生这种情况。在比较感染野生型HSV-1(NS)的细胞和感染FcR缺陷型突变体(ENS)的细胞的实验中,我们证明HSV-1 FcR参与抗体双极桥接会降低抗体依赖性细胞毒性的有效性。