在生理条件下对与人类鼻病毒结合的单个受体分子的可视化。

Visualization of single receptor molecules bound to human rhinovirus under physiological conditions.

作者信息

Kienberger Ferry, Rankl Christian, Pastushenko Vassili, Zhu Rong, Blaas Dieter, Hinterdorfer Peter

机构信息

Institute for Biophysics, J. Kepler University, Altenbergerstrasse 69, A-4040 Linz, Austria.

出版信息

Structure. 2005 Sep;13(9):1247-53. doi: 10.1016/j.str.2005.06.012.

DOI:10.1016/j.str.2005.06.012

PMID:16154082

Abstract

Dynamic force microscopy (DFM) was used to image human rhinovirus HRV2 alone and complexed with single receptor molecules under near physiological conditions. Specific and site-directed immobilization of HRV2 on a model cell membrane resulted in a crystalline arrangement of virus particles with hexagonal symmetry and 35 nm spacing. High-resolution imaging of the virus capsid revealed about 20 resolvable structural features with 3 nm diameters; this finding is in agreement with protrusions seen by cryo-electron microscopy. Binding of receptor molecules to individual virus particles was observed after injection of soluble receptors into the liquid cell. Virus-receptor complexes with zero, one, two, or three attached receptor molecules were resolved. The number of receptor molecules associated to virions increased over time. Occasionally, dissociation of single receptor molecules from viral particles was also observed.

摘要

在接近生理条件下，利用动态力显微镜（DFM）对单独的人鼻病毒HRV2以及与单个受体分子复合的HRV2进行成像。将HRV2特异性地、定点固定在模型细胞膜上，形成了具有六边形对称性且间距为35纳米的病毒颗粒晶体排列。对病毒衣壳的高分辨率成像显示出约20个直径为3纳米的可分辨结构特征；这一发现与冷冻电子显微镜观察到的突起一致。将可溶性受体注入液体池后，观察到受体分子与单个病毒颗粒的结合。分辨出了带有零个、一个、两个或三个附着受体分子的病毒 - 受体复合物。与病毒粒子相关的受体分子数量随时间增加。偶尔也观察到单个受体分子从病毒颗粒上解离。