TY - JOUR T1 - Role of Gag and lipids during HIV-1 assembly in CD4(+) T cells and macrophages A1 - Mariani,Charlotte A1 - Desdouits,Marion A1 - Favard,Cyril A1 - Benaroch,Philippe A1 - Muriaux,Delphine M. AD - Ctr Etude Agents Pathogenes & Biotechnol Sante, CNRS, UMR 5236, F-34293 Montpellier, France. AD - Inst Curie Inserm U932, Paris, France. UR - https://archimer.ifremer.fr/doc/00344/45490/ DO - 10.3389/fmicb.2014.00312 KW - HIV-1 KW - lipids KW - assembly KW - Gag KW - CD4(+) T cells KW - macrophages N2 - HIV-1 is an RNA enveloped virus that preferentially infects CD4(+) T lymphocytes and also macrophages. In CD4(+) T cells, HIV-1 mainly buds from the host cell plasma membrane. The viral Gag polyprotein targets the plasma membrane and is the orchestrator of the HIV assembly as its expression is sufficient to promote the formation of virus-like particles carrying a lipidic envelope derived from the host cell membrane. Certain lipids are enriched in the viral membrane and are thought to play a key role in the assembly process and the envelop composition. A large body of work performed on infected CD4(+) T cells has provided important knowledge about the assembly process and the membrane virus lipid composition. While HIV assembly and budding in macrophages is thought to follow the same general Gag-driven mechanism as in T-lymphocytes, the HIV cycle in macrophage exhibits specific features. In these cells, new virions bud from the limiting membrane of seemingly intracellular compartments, where they accumulate while remaining infectious. These structures are now often referred to as Virus Containing Compartments (VCCs). Recent studies suggest that VCCs represent intracellularly sequestered regions of the plasma membrane, but their precise nature remains elusive. The proteomic and lipidomic characterization of virions produced by T cells or macrophages has highlighted the similarity between their composition and that of the plasma membrane of producer cells, as well as their enrichment in acidic lipids, some components of raft lipids and in tetraspanin-enriched microdomains. It is likely that Gag promotes the coalescence of these components into an assembly platform from which viral budding takes place. How Gag exactly interacts with membrane lipids and what are the mechanisms involved in the interaction between the different membrane nanodomains within the assembly platform remains unclear. Here we review recent literature regarding the role of Gag and lipids on HIV-1 assembly in CD4(+) T cells and macrophages. Y1 - 2014/06 PB - Frontiers Research Foundation JF - Frontiers In Microbiology SN - 1664-302X VL - 5 IS - 312 SP - 1 EP - 9 ID - 45490 ER -