Rankl Christian, Kienberger Ferry, Wildling Linda, Wruss Jürgen, Gruber Hermann J, Blaas Dieter, Hinterdorfer Peter
Institute for Biophysics, Christian Doppler Laboratory for Nanoscopic Methods in Biophysics, University of Linz, Altenbergerstrasse 69, A-4040 Linz, Austria.
Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17778-83. doi: 10.1073/pnas.0806451105. Epub 2008 Nov 7.
Minor group human rhinoviruses (HRVs) attach to members of the low-density lipoprotein receptor family and are internalized via receptor-mediated endocytosis. The attachment of HRV2 to the cell surface, the first step in infection, was characterized at the single-molecule level by atomic force spectroscopy. Sequential binding of multiple receptors was evident from recordings of characteristic quantized force spectra, which suggests that multiple receptors bound to the virus in a timely manner. Unbinding forces required to detach the virus from the cell membrane increased within a time frame of several hundred milliseconds. The number of receptors involved in virus binding was determined, and estimates for on-rate, off-rate, and equilibrium binding constant of the interaction between HRV2 and plasma membrane-anchored receptors were obtained.
微小群人鼻病毒（HRVs）附着于低密度脂蛋白受体家族成员，并通过受体介导的内吞作用内化。HRV2与细胞表面的附着是感染的第一步，通过原子力光谱在单分子水平上进行了表征。从特征性量化力谱记录中明显看出多个受体的顺序结合，这表明多个受体及时与病毒结合。在几百毫秒的时间范围内，将病毒从细胞膜上分离所需的解离力增加。确定了参与病毒结合的受体数量，并获得了HRV2与质膜锚定受体之间相互作用的结合速率、解离速率和平衡结合常数的估计值。
