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

Show full item record



Permalink

http://hdl.handle.net/10138/332610

Citation

Inamdar , K , Tsai , F-C , Dibsy , R , de Poret , A , Manzi , J , Merida , P , Muller , R , Lappalainen , P , Roingeard , P , Mak , J , Bassereau , P , Favard , C & Muriaux , D 2021 , ' Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53 ' , eLife , vol. 10 , 67321 . https://doi.org/10.7554/eLife.67321

Title: Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53
Author: Inamdar, Kaushik; Tsai, Feng-Ching; Dibsy, Rayane; de Poret, Aurore; Manzi, John; Merida, Peggy; Muller, Remi; Lappalainen, Pekka; Roingeard, Philippe; Mak, Johnson; Bassereau, Patricia; Favard, Cyril; Muriaux, Delphine
Other contributor: University of Helsinki, Institute of Biotechnology

Date: 2021-06-11
Language: eng
Number of pages: 26
Belongs to series: eLife
ISSN: 2050-084X
DOI: https://doi.org/10.7554/eLife.67321
URI: http://hdl.handle.net/10138/332610
Abstract: 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.
Subject: COLOCALIZATION ANALYSIS
VIRUS
DOMAIN
CDC42
INHIBITION
MECHANISM
PROTEINS
RELEASE
PATHWAY
BINDING
1182 Biochemistry, cell and molecular biology
Rights:


Files in this item

Total number of downloads: Loading...

Files Size Format View
elife_67321_v2.pdf 3.565Mb PDF View/Open

This item appears in the following Collection(s)

Show full item record