Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53

eLife

Remi Muller¹  Rayane Dibsy²  Aurore de Poret²  Peggy Merida²  Kaushik Inamdar²  Cyril Favard²  Delphine Muriaux²  John Manzi³  Feng-Ching Tsai³  Patricia Bassereau³  Johnson Mak⁴  Pekka Lappalainen⁵  Philippe Roingeard⁶ 

[1] CEMIPAI, CNRS UAR3725, University of Montpellier, Montpellier, France;Infectious disease Research Institute of Montpellier (IRIM), CNRS UMR 9004, University of Montpellier, Montpellier, France;Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico Chimie Curie, Paris, France;Institute for Glycomics, Griffith University, Brisbane, Australia;Institute of Biotechnology, University of Helsinki, Helsinki, Finland;MAVIVH UMR Inserm U1259, University of Tours, Tours, France;

关键词: viruses;    plasma membrane;    single molecule localisation microscopy;   

DOI  :  10.7554/eLife.67321

来源: DOAJ

【 摘 要 】

During HIV-1 particle formation, the requisite plasma membrane curvature is thought to be solely driven by the retroviral Gag protein. Here, we reveal that the cellular I-BAR protein IRSp53 is required for the progression of HIV-1 membrane curvature to complete particle assembly. siRNA-mediated knockdown of IRSp53 gene expression induces a decrease in viral particle production and a viral bud arrest at half completion. Single-molecule localization microscopy at the cell plasma membrane shows a preferential localization of IRSp53 around HIV-1 Gag assembly sites. In addition, we observe the presence of IRSp53 in purified HIV-1 particles. Finally, HIV-1 Gag protein preferentially localizes to curved membranes induced by IRSp53 I-BAR domain on giant unilamellar vesicles. Overall, our data reveal a strong interplay between IRSp53 I-BAR and Gag at membranes during virus assembly. This highlights IRSp53 as a crucial host factor in HIV-1 membrane curvature and its requirement for full HIV-1 particle assembly.

【 授权许可】

Unknown