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Dynamic Association between HIV-1 Gag and Membrane Domains

机译:HIV-1堵嘴与膜结构域之间的动态关联

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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.
机译:HIV-1颗粒的组装由结构蛋白Gag驱动。堵嘴结合并在质膜的内部小叶上聚合,最终导致形成球形颗粒。在病毒在T细胞之间传播期间,Gag会积聚到质膜结构域,与目标细胞膜一起形成称为病毒突触的细胞连接。尽管Gag与质膜微结构域的关联已经牵涉到病毒装配和细胞间传播中,但最近的研究表明,Gag不仅通过积累到预先存在的微结构域,还通过其多聚活性在重组微结构域中发挥了积极作用。在本文中,我们将讨论Gag微域相互作用的这一新兴观点。 Gag多聚化与微域关联之间的关系将在Gag定位到T细胞尾足和病毒突触的背景下进一步讨论。

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