Interaction of the poliovirus receptor with poliovirus
Interaction of the poliovirus receptor with poliovirus
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DOI：
10.1073/pnas.97.1.79
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发表时间：
2000-01-04
影响因子：
11.1
通讯作者：
Rossmann, MG
中科院分区：
文献类型：
--
作者：
He, YN;Bowman, VD;Rossmann, MG
通过冷冻电子显微镜和三维图像重建技术，确定了与脊髓灰质炎病毒（血清型I）复合的细胞外三结构域脊髓灰质炎病毒受体（CD 155）的结构，分辨率为22埃。在差异电子密度图中分离对应于受体的密度，并与已知结构拟合，与三个单独的CD 155 Ig样结构域的结构同源。通过CD 155糖蛋白中碳水化合物部分的位置、具有Ig样折叠的细胞表面分子结构中肘角的保守性质以及与先前CD 155和脊髓灰质炎病毒诱变结果的一致性证实了该拟合。CD 155在脊髓灰质炎病毒“峡谷”中结合，并且具有与人鼻病毒上的细胞间粘附分子-1受体相似的足迹。然而，细长的CD 155分子相对于脊髓灰质炎病毒表面的取向与鼻病毒上细胞间粘附分子-1的取向完全不同。此外，提供识别特异性的残基对于两种受体不同。这两种小核糖核酸病毒共同的受体结合的主要特征是结合发生在峡谷中的位点。该位点可能是启动病毒感染所需的后续去包被步骤的触发因素。
The structure of the extracellular, three-domain poliovirus receptor (CD155) complexed with poliovirus (serotype I)has been determined to 22-Angstrom resolution by means of cryo-electron microscopy and three-dimensional image-reconstruction techniques. Density corresponding to the receptor was isolated in a difference electron density map and fitted with known structures, homologous to those of the three individual CD155 Ig-like domains. The fit was confirmed by the location of carbohydrate moieties in the CD155 glycoprotein, the conserved properties of elbow angles in the structures of cell surface molecules with Ig-like folds, and the concordance with prior results of CD155 and poliovirus mutagenesis. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. However, the orientation of the long, slender CD155 molecule relative to the poliovirus surface is quite different from the orientation of intercellular adhesion molecule-1 on rhinoviruses. In addition, the residues that provide specificity of recognition differ for the two receptors. The principal feature of receptor binding common to these two picornaviruses is the site in the canyon at which binding occurs. This site may be a trigger for initiation of the subsequent uncoating step required for viral infection.