• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Retroviral capsid assembly: a role for the CA dimer in initiation.
【24h】

Retroviral capsid assembly: a role for the CA dimer in initiation.

机译：逆转录病毒衣壳装配：CA二聚体在启动中的作用。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

In maturing retroviral virions, CA protein assembles to form a capsid shell that is essential for infectivity. The structure of the two folded domains [N-terminal domain (NTD) and C-terminal domain (CTD)] of CA is highly conserved among various retroviruses, and the capsid assembly pathway, although poorly understood, is thought to be conserved as well. In vitro assembly reactions with purified CA proteins of the Rous sarcoma virus (RSV) were used to define factors that influence the kinetics of capsid assembly and provide insights into underlying mechanisms. CA multimerization was triggered by multivalent anions providing evidence that in vitro assembly is an electrostatically controlled process. In the case of RSV, in vitro assembly was a well-behaved nucleation-driven process that led to the formation of structures with morphologies similar to those found in virions. Isolated RSV dimers, when mixed with monomeric protein, acted as efficient seeds for assembly, eliminating the lag phase characteristic of a monomer-only reaction. This demonstrates for the first time the purification of an intermediate on the assembly pathway. Differences in the intrinsic tryptophan fluorescence of monomeric protein and the assembly-competent dimer fraction suggest the involvement of the NTD in the formation of the functional dimer. Furthermore, in vitro analysis of well-characterized CTD mutants provides evidence for assembly dependence on the second domain and suggests that the establishment of an NTD-CTD interface is a critical step in capsid assembly initiation. Overall, the data provide clear support for a model whereby capsid assembly within the maturing virion is dependent on the formation of a specific nucleating complex that involves a CA dimer and is directed by additional virion constituents.
机译：在成熟的逆转录病毒颗粒中，CA蛋白组装形成衣壳，这对于感染至关重要。在两种逆转录病毒中，CA的两个折叠结构域[N末端结构域（NTD）和C末端结构域（CTD）]的结构高度保守，衣壳装配途径尽管知之甚少，但也被认为是保守的。 。与劳斯肉瘤病毒（RSV）纯化的CA蛋白的体外装配反应用于定义影响衣壳装配动力学的因素，并提供对潜在机制的了解。 CA多聚是由多价阴离子触发的，提供了体外组装是静电控制过程的证据。就RSV而言，体外组装是一个表现良好的成核驱动过程，导致形成具有类似于病毒粒子的形态的结构。分离的RSV二聚体与单体蛋白混合后，可作为有效的组装种子，消除了仅单体反应的滞后特性。这首次证明了组装路径上中间体的纯化。单体蛋白的固有色氨酸荧光和具有装配能力的二聚体组分之间的差异表明NTD参与了功能性二聚体的形成。此外，对特征明确的CTD突变体的体外分析为装配依赖第二域提供了证据，并表明NTD-CTD接口的建立是衣壳装配启动的关键步骤。总体而言，数据为模型提供了明确的支持，在该模型中，成熟病毒体中的衣壳组装取决于特定的成核复合物的形成，该复合物涉及CA二聚体，并由其他病毒体成分控制。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号