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I型脊髓灰质炎病毒萨宾株的热敏性阻断

Thermosensitive block of the Sabin strain of poliovirus type I.

作者信息

Fiszman M, Reynier M, Bucchini D, Girard M

出版信息

J Virol. 1972 Dec;10(6):1143-51. doi: 10.1128/JVI.10.6.1143-1151.1972.

Abstract

The thermosensitive defect of the Sabin LSc2ab strain of poliovirus type I was studied. Transfer of infected KB cells from 36 to 38.5 C resulted in 30% inhibition of viral RNA replication but in 90% inhibition of formation of virions. Neither 74S procapsids nor 14S particles were detected in the cells transferred to the non-permissive temperature. However, procapsids, once accumulated at 36 C, were normally stable at 38.5 C and could transform into virions at that temperature. Viral proteins synthesized at the nonpermissive temperature were not different from those synthesized at permissive temperature, as judged from their pattern in polyacrylamide gel electrophoresis and from the fact that they normally matured into virions when the infected cells were brought back to permissive temperature, even under conditions of inhibition of protein synthesis. This leads to the conclusion that the defect in the Sabin strain studied lies in the assembly of its viral capsid proteins into capsomeres.

摘要

对I型脊髓灰质炎病毒的Sabin LSc2ab株的热敏缺陷进行了研究。将感染的KB细胞从36℃转移至38.5℃导致病毒RNA复制受到30%的抑制,但病毒粒子形成受到90%的抑制。在转移至非允许温度的细胞中未检测到74S原衣壳和14S颗粒。然而,原衣壳一旦在36℃积累,在38.5℃时通常是稳定的,并且可以在该温度下转化为病毒粒子。从聚丙烯酰胺凝胶电泳图谱以及即使在蛋白质合成受到抑制的条件下,当感染细胞回到允许温度时它们通常会成熟为病毒粒子这一事实判断,在非允许温度下合成的病毒蛋白与在允许温度下合成的病毒蛋白没有差异。这得出结论,所研究的Sabin株的缺陷在于其病毒衣壳蛋白组装成壳粒。

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