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Saturable binding sites for vesicular stomatitis virus on the surface of Vero cells.

机译:Vero细胞表面上水泡性口炎病毒的饱和结合位点。

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摘要

The binding of vesicular stomatitis virus (VSV) to Vero monkey cells was studied by using virus metabolically labeled with [35S]methionine. Under conditions where viral uptake did not occur (4 degrees C), apparent binding equilibrium was achieved within 12 h at a level representing 12% of the input virus. Two distinct forms of virus-cell interaction were found. At low concentrations of VSV, corresponding to multiplicities used for tissue culture studies, saturable binding was the major form of interaction. Saturation was complete at approximately 4,000 VSV virions per cell. At higher virus concentrations, nonsaturable binding prevailed. Trypsin treatment of Vero cells did not decrease the binding of VSV to the saturable binding sites. Internalization of VSV at 37 degrees C also displayed a saturable component which was directly comparable to that observed for binding. VSV binding to high-affinity, saturable sites on the plasma membrane may represent a receptor-mediated route of viral uptake.
机译:用[35S]蛋氨酸代谢标记的病毒研究了水泡性口炎病毒(VSV)与Vero猴细胞的结合。在未发生病毒摄取的条件下(4摄氏度),在12小时内达到了代表输入病毒12%的水平的明显结合平衡。发现了两种不同形式的病毒-细胞相互作用。在低浓度的VSV下,与用于组织培养研究的多重性相对应,饱和结合是相互作用的主要形式。每个细胞约4,000个VSV病毒体饱和。在较高的病毒浓度下,不饱和结合占主导。胰蛋白酶处理Vero细胞不会降低VSV与可饱和结合位点的结合。在37摄氏度时,VSV的内在化也显示出可饱和的成分,该成分与观察到的结合具有可比性。 VSV结合到质膜上的高亲和力,饱和位点可能代表受体介导的病毒摄取途径。

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