Rossmann M G
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392.
Protein Sci. 1994 Oct;3(10):1712-25. doi: 10.1002/pro.5560031010.
Rhinovirus infection is initiated by the recognition of a specific cell-surface receptor. The major group of rhinovirus serotypes attach to intercellular adhesion molecule-1 (ICAM-1). The attachment process initiates a series of conformational changes resulting in the loss of genomic RNA from the virion. X-ray crystallography and sequence comparisons suggested that a deep crevice or canyon is the site on the virus recognized by the cellular receptor molecule. This has now been verified by electron microscopy of human rhinovirus 14 (HRV14) and HRV16 complexed with a soluble component of ICAM-1. A hydrophobic pocket underneath the canyon is the site of binding of various hydrophobic drug compounds that can inhibit attachment and uncoating. This pocket is also associated with an unidentified, possibly cellular in origin, "pocket factor." The pocket factor binding site overlaps the binding site of the receptor. It is suggested that competition between the pocket factor and receptor regulates the conformational changes required for the initiation of the entry of the genomic RNA into the cell.
鼻病毒感染是由对特定细胞表面受体的识别引发的。主要的鼻病毒血清型群与细胞间黏附分子-1（ICAM-1）结合。附着过程引发一系列构象变化，导致病毒粒子中的基因组RNA丢失。X射线晶体学和序列比较表明，一个深裂缝或峡谷是病毒上被细胞受体分子识别的位点。这一点现已通过人鼻病毒14（HRV14）和HRV16与ICAM-1的可溶性成分复合的电子显微镜观察得到证实。峡谷下方的一个疏水口袋是各种可抑制附着和解衣壳的疏水药物化合物的结合位点。这个口袋还与一种身份不明、可能起源于细胞的“口袋因子”相关。口袋因子结合位点与受体的结合位点重叠。有人提出，口袋因子与受体之间的竞争调节了基因组RNA进入细胞起始所需的构象变化。
