Yang Xinzhen, Lipchina Inna, Cocklin Simon, Chaiken Irwin, Sodroski Joseph
Beth Israel Deaconess Medical Center, 330 Brookline Avenue, R.E. 213A, Boston, MA 02215, USA.
J Virol. 2006 Nov;80(22):11404-8. doi: 10.1128/JVI.01102-06. Epub 2006 Sep 6.
Primary and laboratory-adapted variants of human immunodeficiency virus type 1 (HIV-1) exhibit a wide range of sensitivities to neutralization by antibodies directed against the viral envelope glycoproteins. An antibody directed against an artificial FLAG epitope inserted into the envelope glycoproteins of three HIV-1 isolates with vastly different neutralization sensitivities inhibited all three viruses equivalently. Thus, naturally occurring HIV-1 isolates that are neutralization resistant are not necessarily more impervious to the inhibitory consequences of bound antibody. Moreover, the binding affinity of the anti-FLAG antibody correlated with neutralizing potency, underscoring the dominant impact on neutralization of antibody binding to the envelope glycoproteins.
1型人类免疫缺陷病毒（HIV-1）的原始毒株和实验室适应性变体对针对病毒包膜糖蛋白的抗体中和作用表现出广泛的敏感性。一种针对插入到三种具有截然不同中和敏感性的HIV-1分离株包膜糖蛋白中的人工FLAG表位的抗体，能同等程度地抑制这三种病毒。因此，具有中和抗性的天然HIV-1分离株不一定对结合抗体的抑制作用更具抗性。此外，抗FLAG抗体的结合亲和力与中和效力相关，突出了抗体与包膜糖蛋白结合对中和作用的主要影响。
