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首页> 外文期刊>Biochemistry >Attachment of VLDL Receptors to an Icosahedral Virus along the 5-fold Symmetry Axis: Multiple Binding Modes Evidenced by Fluorescence Correlation Spectroscopy
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Attachment of VLDL Receptors to an Icosahedral Virus along the 5-fold Symmetry Axis: Multiple Binding Modes Evidenced by Fluorescence Correlation Spectroscopy

机译：沿5倍对称轴将VLDL受体附着于二十面体病毒：荧光相关光谱法证明的多种结合模式。

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摘要

Human rhinoviruses (HRVs) are composed of 60 identical subunits, each comprising one copy of the viral capsid proteins VP1, 2, 3, and 4. Consequently, 60 symmetry-related epitopes are available for binding of antibodies or receptors. The minor receptor group of HRVs uses members of the low-density lipoprotein receptor family for cell entry. The ligand binding domains of these receptors are composed of various numbers of ligand binding repeats, and several of these modules within a single molecule are believed to attach simultaneously to the star-shaped dome at the 5-fold symmetry axis of the virus. Using fluorescence correlation spectroscopy (FCS), we have now determined the equilibrium binding constants and the mode of attachment of recombinant concatemers of ligand binding module 3 of the human very-low-density lipoprotein receptor to HRV2. We demonstrate that the avidity of the interaction drastically increases with the number of concatenated modules. For the trimer, the binding isotherm was biphasic, indicating that attachment of two and of three modules within the same molecule was resolved. The receptor consisting of seven repeats was found to bind most strongly, but a complete binding isotherm could not be established due to cross-linking of virions. The values of the dissociation constants were about 1 order of magnitude higher than those previously determined by using surface plasmon resonance techniques reflecting the different presentation of the binding partners. As compared to the concatemers, the natural receptors are composed of similar but not identical repeats; thus, cooperativity and different specificity of the ligand-binding modules allow for recognition of many ligands and viral serotypes. Due to the low concentrations and amounts of sample required, FCS is ideally suited for the determination of receptor binding parameters of viruses difficult to produce in high quantities and/or concentrations.
机译：人鼻病毒（HRV）由60个相同的亚基组成，每个亚基均包含病毒衣壳蛋白VP1、2、3和4的一个副本。因此，有60个与对称性有关的表位可用于抗体或受体的结合。 HRV的次要受体群使用低密度脂蛋白受体家族的成员进入细胞。这些受体的配体结合结构域由各种数量的配体结合重复序列组成，单个分子中的多个模块被认为在病毒的5倍对称轴上同时附着在星形圆顶上。使用荧光相关光谱法（FCS），我们现在已经确定了人类非常低密度脂蛋白受体的配体结合模块3的重组连接体与HRV2的平衡结合常数和连接模式。我们证明了相互作用的亲和力随着级联模块的数量急剧增加。对于三聚体，结合等温线是双相的，表明在同一分子内两个和三个模块的连接已分解。发现由七个重复序列组成的受体结合最牢固，但是由于病毒体的交联而不能建立完全的结合等温线。离解常数的值比先前通过使用表面等离振子共振技术测定的那些反映结合配体的不同呈现方式的值高约1个数量级。与串联体相比，天然受体由相似但不相同的重复组成。因此，配体结合模块的协同作用和不同的特异性可以识别许多配体和病毒血清型。由于所需样品的浓度低和量少，FCS非常适合确定难以大量生产和/或浓缩的病毒的受体结合参数。

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