Selinka H C, Zibert A, Wimmer E
Department of Microbiology, State University of New York, Stony Brook 11794.
Proc Natl Acad Sci U S A. 1991 May 1;88(9):3598-602. doi: 10.1073/pnas.88.9.3598.
Mouse fibroblast cell lines were transfected with truncated forms of the human poliovirus receptor (PVR) cDNA and tested for the expression of functional receptors for poliovirus. Several receptor constructs, all containing the coding region of the first 143 amino acids of PVR, were able to render mouse cells susceptible to poliovirus infection. A deletion of 65 amino acids in the first extracellular domain of PVR prevented virus attachment and infection. These data suggest that domain 1 is necessary and sufficient for the virus-receptor interaction. A PVR/intercellular adhesion molecule 1 hybrid receptor, expressing the PVR variable domain on a truncated receptor molecule for human rhinovirus 14, was shown to be a functional receptor for poliovirus. This observation indicates that, subsequent to attachment to the PVR-binding domain, poliovirus can use the same pathway as the major receptor group rhinoviruses to enter cells.
用截短形式的人脊髓灰质炎病毒受体（PVR）cDNA转染小鼠成纤维细胞系，并检测其对脊髓灰质炎病毒功能性受体的表达。几种受体构建体，均包含PVR前143个氨基酸的编码区，能够使小鼠细胞易受脊髓灰质炎病毒感染。PVR第一个细胞外结构域缺失65个氨基酸会阻止病毒附着和感染。这些数据表明结构域1对于病毒-受体相互作用是必要且充分的。一种PVR/细胞间粘附分子1杂交受体，在人鼻病毒14的截短受体分子上表达PVR可变结构域，被证明是脊髓灰质炎病毒的功能性受体。这一观察结果表明，在附着于PVR结合结构域之后，脊髓灰质炎病毒可以利用与主要受体组鼻病毒相同的途径进入细胞。
