STRUCTURE OF A HUMAN RHINOVIRUS BIVALENTLY BOUND ANTIBODY COMPLEX - IMPLICATIONS FOR VIRAL NEUTRALIZATION AND ANTIBODY FLEXIBILITY
STRUCTURE OF A HUMAN RHINOVIRUS BIVALENTLY BOUND ANTIBODY COMPLEX - IMPLICATIONS FOR VIRAL NEUTRALIZATION AND ANTIBODY FLEXIBILITY
复制标题
DOI：
10.1073/pnas.90.15.7015
复制
发表时间：
1993-08-01
影响因子：
11.1
通讯作者：
BAKER, TS
中科院分区：
文献类型：
--
作者：
SMITH, TJ;OLSON, NH;BAKER, TS
结合人鼻病毒14（HRV 14）的中和免疫球蛋白（单克隆抗体mAb 17-IA）的结构已通过冷冻电子显微镜和图像重建确定。该抗体结合的双抗体跨越病毒的二十面体双重轴，并且在衣壳中没有可检测到的构象变化。因此，双抗体结合的IgG似乎不会引起衣壳的总体变形。结合的Fab片段和IgG结构的恒定结构域的电子密度之间的差异表明，如先前预测的那样，在二价连接后，围绕肘轴发生构象变化。Fc片段未观察到显著密度，这进一步证明了铰链区周围的高度移动性。
The structure of a neutralizing immunoglobulin (monoclonal antibody mAb17-IA), bound to human rhinovirus 14 (HRV14), has been determined by cryo-electron microscopy and image reconstruction. The antibody bound bivalently across icosahedral twofold axes of the virus, and there were no detectable conformational changes in the capsid. Thus, bivalently bound IgGs do not appear to cause gross deformations in the capsid. Differences between the electron density of the constant domains of the bound Fab fragment and IgG structures suggested that conformational changes occur about elbow axes upon bivalent attachment as was previously predicted. No significant density was observed for the Fc fragment, which adds further evidence for a high degree of mobility about the hinge region.