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引用次数: 0
摘要
HIV-1 颗粒的组装是由结构蛋白 Gag 驱动的。Gag 与质膜内叶结合并多聚化,最终形成球形颗粒。在病毒在 T 细胞间传播的过程中,Gag 会聚集到质膜结构域,该结构域与靶细胞膜一起形成一个称为病毒突触的细胞连接点。虽然 Gag 与质膜微域的结合与病毒的组装和细胞间的传播有关,但最近的研究表明,Gag 不仅仅积聚在已存在的微域,还通过其多聚化活性在重组微域方面发挥着积极作用。本文将讨论这种关于 Gag 微域相互作用的新观点。我们还将结合 Gag 在 T 细胞尿囊和病毒突触中的定位进一步讨论 Gag 多聚化与微域关联之间的关系。
Dynamic Association between HIV-1 Gag and Membrane Domains.
HIV-1 particle assembly is driven by the structural protein Gag. Gag binds to and multimerizes on the inner leaflet of the plasma membrane, eventually resulting in formation of spherical particles. During virus spread among T cells, Gag accumulates to the plasma membrane domain that, together with target cell membrane, forms a cell junction known as the virological synapse. While Gag association with plasma membrane microdomains has been implicated in virus assembly and cell-to-cell transmission, recent studies suggest that, rather than merely accumulating to pre-existing microdomains, Gag plays an active role in reorganizing the microdomains via its multimerization activity. In this paper, we will discuss this emerging view of Gag microdomain interactions. Relationships between Gag multimerization and microdomain association will be further discussed in the context of Gag localization to T-cell uropods and virological synapses.