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

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 knoc...

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Published ineLife Vol. 10
Main Authors 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
Format Journal Article
LanguageEnglish
Published Cambridge eLife Science Publications, Ltd 11.06.2021
eLife Sciences Publications Ltd
eLife Sciences Publication
eLife Sciences Publications, Ltd
Subjects
BAR protein
Biochemistry, Molecular Biology
Biophysics
Cellular Biology
Condensed Matter
Experiments
Gag protein
Gene expression
HIV
Human immunodeficiency virus
Kinases
Life Sciences
Localization
Lymphocytes
Pathogens
Physics
Physics of Living Systems
Plasma
plasma membrane
Proteins
single molecule localisation microscopy
siRNA
Soft Condensed Matter
Subcellular Processes
Transmission electron microscopy
Viruses
Fiji
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Summary: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.
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ORCID: 0000-0002-8304-2980.
ISSN:2050-084X
2050-084X
DOI:10.7554/eLife.67321