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HIV-1 核衣壳蛋白与膜结构域之间的动态关联

Dynamic Association between HIV-1 Gag and Membrane Domains.

作者信息

Hogue Ian B, Llewellyn G Nicholas, Ono Akira

机构信息

Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.

出版信息

Mol Biol Int. 2012;2012:979765. doi: 10.1155/2012/979765. Epub 2012 Jul 5.

Abstract

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.

摘要

HIV-1病毒颗粒的组装由结构蛋白Gag驱动。Gag与质膜的内小叶结合并多聚化,最终导致球形颗粒的形成。在病毒在T细胞中传播期间,Gag积累到质膜区域,该区域与靶细胞膜一起形成称为病毒突触的细胞连接。虽然Gag与质膜微结构域的结合与病毒组装和细胞间传播有关,但最近的研究表明,Gag并非仅仅积累到预先存在的微结构域,而是通过其多聚化活性在微结构域的重组中发挥积极作用。在本文中,我们将讨论这种关于Gag与微结构域相互作用的新观点。Gag多聚化与微结构域结合之间的关系将在Gag定位于T细胞尾足和病毒突触的背景下进一步讨论。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3c27/3399408/e902ff8a6b30/MBI2012-979765.001.jpg

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