Poliovirus binding to its receptor in lipid bilayers results in particle-specific, temperature-sensitive channels.
Poliovirus binding to its receptor in lipid bilayers results in particle-specific, temperature-sensitive channels.
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脊髓灰质炎病毒与其脂质双层中的受体结合，形成颗粒特异性、温度敏感的通道。
DOI：
10.1099/vir.0.19745-0
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发表时间：
2004
期刊：
影响因子：
--
通讯作者：
Chow,Marie
中科院分区：
文献类型：
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作者：
Tosteson,MagdalenaT;Wang,Hong;Naumov,Anatoli;Chow,Marie
脊髓灰质炎病毒（PV）感染开始于与其受体（PVR）结合，随后是感染性颗粒（在160 S时沉降）的受体辅助的温度敏感性构象变化，变为在135 S时沉降的颗粒。在这次通信中报告的是成功地纳入脂质双层的两种形式的受体：全长的人受体和修饰的克隆，其中受体的胞外结构域融合到糖基磷脂酰肌醇尾巴。将病毒（160 S）加入到含有受体的双层中导致通道形成，而当加入受体修饰的病毒颗粒（135 S）时没有观察到通道。将温度从21 °C增加到31 °C导致单通道电导的幅度增加10倍，这可以解释为通道结构的构象变化。 一个突变的PV与氨基酸的变化在VP 4（外壳蛋白之一），这是在基因组脱壳缺陷不能产生通道，这表明VP 4可能参与通道结构。这些研究提供了脊髓灰质炎病毒与其受体结合到脂质双层膜之间的相互作用的第一个电生理表征。此外，它们为未来旨在定义病毒-受体复合物的分子结构的研究奠定了基础。
Poliovirus (PV) infection starts with binding to its receptor (PVR), followed by a receptor-aided, temperature-sensitive conformational change of the infectious particle (sedimenting at 160S) to a particle which sediments at 135S. Reported in this communication is the successful incorporation into lipid bilayers of two forms of the receptor: the full-length human receptor and a modified clone in which the extracellular domains of the receptor were fused to a glycosylphosphatidylinositol tail. Addition of virus (160S) to receptor-containing bilayers leads to channel formation, whereas no channels were observed when the receptor-modified viral particle (135S) was added. Increasing the temperature from 21 to 31 °C led to a 10-fold increase in the magnitude of the single channel conductance, which can be interpreted as a conformational change in the channel structure. A mutant PV with an amino acid change in VP4 (one of the coat proteins) which is defective in genome uncoating failed to produce channels, suggesting that VP4 might be involved in the channel architecture. These studies provide the first electrophysiological characterization of the interactions between poliovirus and its receptor incorporated into a lipid bilayer membrane. Furthermore, they form the foundation for future studies aiming at defining the molecular architecture of the virus–receptor complex.