Department of Chemical Research Support, Israel.
Ultramicroscopy. 2010 May;110(6):694-700. doi: 10.1016/j.ultramic.2010.02.034. Epub 2010 Mar 16.
One of the most important steps in the process of viral infection is a fusion between cell membrane and virus, which is mediated by the viral envelope glycoprotein. The study of activity of the glycoprotein in the post-fusion state is important for understanding the progression of infection. Here we present a first real-time kinetic study of the activity of gp41 (the viral envelope glycoprotein of human immunodeficiency virus-HIV) and its two mutants in the post-fusion state with nanometer resolution by atomic force microscopy (AFM). Tracking the changes in the phosphatidylcholine (PC) and phosphatidylcholine-phosphatidylserine (PC:PS) membrane integrity over one hour by a set of AFM images revealed differences in the interaction of the three types of protein with zwitterionic and negatively charged membranes. A quantitative analysis of the slow kinetics of hole formation in the negatively charged lipid bilayer is presented. Specifically, analysis of the rate of roughness change for the three types of proteins suggests that they exhibit different types of kinetic behavior.
病毒感染过程中最重要的步骤之一是细胞膜与病毒之间的融合，这是由病毒包膜糖蛋白介导的。研究融合后糖蛋白的活性对于了解感染的进展非常重要。在这里，我们通过原子力显微镜（AFM）以纳米分辨率首次实时研究了 HIV 病毒包膜糖蛋白 gp41 及其两种突变体在融合后的活性。通过一组 AFM 图像跟踪一小时内磷脂酰胆碱（PC）和磷脂酰胆碱-磷脂酰丝氨酸（PC:PS）膜完整性的变化，揭示了三种蛋白与两性离子和带负电荷的膜相互作用的差异。提出了对带负电荷脂质双层中孔形成慢动力学的定量分析。具体而言，对三种蛋白的粗糙度变化率的分析表明，它们表现出不同类型的动力学行为。
