呼肠孤病毒外衣壳蛋白σ3和μ1的结合会引起构象变化，使σ3对蛋白酶敏感。
Association of reovirus outer capsid proteins sigma 3 and mu 1 causes a conformational change that renders sigma 3 protease sensitive.
作者信息
Shepard D A, Ehnstrom J G, Schiff L A
机构信息
Department of Microbiology, University of Minnesota, Minneapolis 55455, USA.
出版信息
J Virol. 1995 Dec;69(12):8180-4. doi: 10.1128/JVI.69.12.8180-8184.1995.
Abstract
Association of the reovirus proteins sigma 3 and mu 1 influences viral entry, initiation of outer capsid assembly, and modulation of the effect of sigma 3 on cellular translation. In this study, we have addressed whether structural changes occur in sigma 3 as a result of its interaction with mu 1. Using differences in protease sensitivity to detect conformationally distinct forms of sigma 3, we showed that association of sigma 3 with mu 1 caused a conformational change in sigma 3 that converted it from a protease-resistant to a protease-sensitive structure and occurred posttranslationally. The effect of mu 1 on the structure of sigma 3 was stoichiometric. Our results are consistent with a model in which sigma 3's association with mu 1 shifts its function from translational control to assembly of an outer capsid in which sigma 3 is folded into the protease-sensitive conformation that is required for its cleavage during the next round of infection.
摘要
呼肠孤病毒蛋白σ3和μ1之间的相互作用会影响病毒进入、外衣壳组装起始以及σ3对细胞翻译作用的调节。在本研究中，我们探讨了σ3与其与μ1相互作用是否会导致其结构变化。利用蛋白酶敏感性差异来检测构象不同的σ3形式，我们发现σ3与μ1的结合导致了σ3的构象变化，使其从蛋白酶抗性结构转变为蛋白酶敏感性结构，且这种变化发生在翻译后。μ1对σ3结构的影响是化学计量的。我们的结果与这样一个模型一致，即σ3与μ1的结合将其功能从翻译控制转变为外衣壳组装，其中σ3折叠成蛋白酶敏感性构象，这是其在下一轮感染期间被切割所必需的。
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