SATURABLE BINDING-SITES MEDIATE THE ENTRY OF AFRICAN SWINE FEVER VIRUS INTO VERO CELLS
SATURABLE BINDING-SITES MEDIATE THE ENTRY OF AFRICAN SWINE FEVER VIRUS INTO VERO CELLS
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DOI：
10.1016/0042-6822(89)90281-x
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发表时间：
1989-02-01
期刊：
影响因子：
3.7
通讯作者：
VINUELA, E
中科院分区：
文献类型：
--
作者：
ALCAMI, A;CARRASCOSA, AL;VINUELA, E
3h标记的非洲猪瘟病毒与敏感的VERO细胞的结合实验表明，非洲猪瘟病毒的结合位点存在于质膜上。平衡结合数据的Scatchard分析表明，每个细胞存在约104个细胞受体位点，解离常数（Kd）为70 pM。病毒进入VERO细胞是由饱和成分介导的，因为非洲猪瘟病毒饱和结合和摄取与相同数量的未标记病毒竞争。类似地，早期病毒蛋白的合成和病毒的产生也被紫外线灭活病毒的浓度所抑制，这些病毒与饱和结合位点上的病毒相竞争，这表明特异性受体介导了非洲猪瘟病毒颗粒的进入，从而在VERO细胞中引发了生产性感染。非洲猪瘟病毒与病毒抗性L细胞的结合不是通过饱和结合位点介导的。由于非饱和相互作用，病毒无法进入L细胞，并且既没有检测到早期病毒蛋白合成，也没有检测到病毒DNA合成，这表明缺乏非洲猪瘟病毒特异性受体是决定L细胞对感染产生抗性的一个因素。
Binding experiments of 3H-labeled African swine fever virus to susceptible VERO cells have shown the presence of the binding sites for African swine fever virus on the plasma membrane. The Scatchard analysis of the binding data at equilibrium indicates the existence of about 104 cellular receptor sites per cell with a dissociation constant (Kd) of 70 pM. Virus entry into VERO cells is mediated by a saturable component, since tritiated African swine fever virus saturable binding and uptake were competed by the same amounts of unlabeled virus. Similarly early viral protein synthesis and virus production were inhibited by concentrations of uv-inactivated virus that competed virus attachment to saturable binding sites, suggesting that specific receptors mediate the entry of African swine fever virus particles that initiate a productive infection in VERO cells. African swine fever virus binding to virus-resistant L cells was not mediated by saturable binding sites. As a result of the nonsaturable interaction the virus was not able to enter L cells and neither early viral protein synthesis nor viral DNA synthesis was detected, indicating that the absence of specific receptors for African swine fever virus is a factor that determines the resistance of L cells to the infection.