Mengovirus的结构和生理特性：无毒、血凝缺陷型突变体表达改变的α(1 D)蛋白且吸附缺陷。
Structural and physiological properties of mengovirus: avirulent, hemagglutination-defective mutants express altered alpha (1 D) proteins and are adsorption-defective.
作者信息
Anderson K, Bond C W
出版信息
Arch Virol. 1987;93(1-2):13-29. doi: 10.1007/BF01313891.
Structural and physiological properties of two mutants of mengovirus, 205 and 280, were compared to those of wild-type virus to understand the molecular basis of changes exhibited in their biological function. Two dimensional gel electrophoresis of wild-type and mutant structural proteins revealed alterations in the isoelectric character of the alpha (1 D) protein of both mutant 205 and 280. These data suggest that alterations in the alpha (1 D) protein may be responsible for the phenotypic changes by the mutants. A delay in detectable virus-specified protein synthesis was exhibited in mutant-infected cells in comparison to wild-type. The amount of RNA synthesized in mutant- and revertant-infected cells was less than that synthesized in wild-type infected cells. Changes in virus-specified macromolecular synthesis in mutant and revertant-infected cells reflected a decrease in the ability of the viruses to attach to cells.
将脑心肌炎病毒的两种突变体205和280的结构和生理特性与野生型病毒的特性进行比较，以了解它们生物学功能中表现出的变化的分子基础。野生型和突变体结构蛋白的二维凝胶电泳显示，突变体205和280的α（1D）蛋白的等电特性发生了改变。这些数据表明，α（1D）蛋白的改变可能是突变体表型变化的原因。与野生型相比，突变体感染的细胞中可检测到的病毒特异性蛋白合成出现延迟。突变体和回复体感染的细胞中合成的RNA量少于野生型感染的细胞。突变体和回复体感染的细胞中病毒特异性大分子合成的变化反映出病毒附着细胞能力的下降。
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