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HIV-1 Budding

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Advances in HIV-1 Assembly and Release

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Abstract

HIV-1 exits infected cells by budding from the plasma membrane, which generates membranous bud necks that must be cleaved in order to yield extracellular virions. To facilitate the fission of the bud necks, HIV-1 engages the cellular endosomal sorting complex required for transport (ESCRT) machinery through so-called late assembly domains in Gag. The viral late domains serve as docking sites for upstream components of the ESCRT pathway. These components are TSG101/ESCRT-I, which binds to the primary HIV-1 late domain, and ALIX, which plays an auxiliary role in HIV-1 budding. The recruitment of upstream ESCRT components to HIV-1 budding sites ultimately leads to the transient assembly of the late-acting ESCRT-III complex. ESCRT-III constitutes the main engine for HIV-1 bud neck cleavage, and for membrane cleavage events during cytokinesis and the budding of intralumenal vesicles into multivesicular bodies. However, surprisingly few ESCRT-III components are essential for HIV-1 release, indicating that the mechanism of HIV-1 bud neck cleavage differs in crucial aspects from the manner in which ESCRT-III carries out cellular abscission events.

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  1. Umass Medical School, LRB 526, 364 Plantation Street, Worcester, MA, 01605, USA

    Heinrich Göttlinger M.D.

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  1. HIV Drug Resistance Program, National Cancer Institute-Frederick, Bg. 535/Rm. 108, Frederick, 21702-1201, Maryland, USA

    Eric O. Freed

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Göttlinger, H. (2013). HIV-1 Budding. In: Freed, E. (eds) Advances in HIV-1 Assembly and Release. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-7729-7_5

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