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

Kaushik Inamdar, Feng-Ching Tsai, Aurore de Poret, Rayane Dibsy, John Manzi, Peggy Merida, Remi Muller, View ORCID ProfilePekka Lappalainen, Philippe Roingeard, Johnson Mak, Patricia Bassereau, Cyril Favard, Delphine Muriaux
doi: https://doi.org/10.1101/2021.02.10.430663
Kaushik Inamdar
1Montpellier Infectious Disease Research Institute (IRIM), CNRS-Université Montpellier, 1919, route de Mende, 34293 Montpellier Cedex, France
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Feng-Ching Tsai
2Laboratoire Physico-Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France
3Sorbonne Université, 75005, Paris, France
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Aurore de Poret
1Montpellier Infectious Disease Research Institute (IRIM), CNRS-Université Montpellier, 1919, route de Mende, 34293 Montpellier Cedex, France
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Rayane Dibsy
1Montpellier Infectious Disease Research Institute (IRIM), CNRS-Université Montpellier, 1919, route de Mende, 34293 Montpellier Cedex, France
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John Manzi
2Laboratoire Physico-Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France
3Sorbonne Université, 75005, Paris, France
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Peggy Merida
1Montpellier Infectious Disease Research Institute (IRIM), CNRS-Université Montpellier, 1919, route de Mende, 34293 Montpellier Cedex, France
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Remi Muller
4CEMIPAI, University of Montpellier, UMS3725 CNRS, Montpellier, France
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Pekka Lappalainen
5Institute of Biotechnology, University of Helsinki, Helsinki, Finland
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  • ORCID record for Pekka Lappalainen
Philippe Roingeard
6MAVIVH, UMR Inserm U1259, University of Tours, Tours, France
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Johnson Mak
7Institute for Glycomics, Griffith University Gold Coast, Southport, QLD, Australia
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Patricia Bassereau
2Laboratoire Physico-Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France
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Cyril Favard
1Montpellier Infectious Disease Research Institute (IRIM), CNRS-Université Montpellier, 1919, route de Mende, 34293 Montpellier Cedex, France
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Delphine Muriaux
1Montpellier Infectious Disease Research Institute (IRIM), CNRS-Université Montpellier, 1919, route de Mende, 34293 Montpellier Cedex, France
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  • For correspondence: delphine.muriaux@irim.cnrs.fr
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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. Partial gene editing of IRSp53 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 localizes preferentially to IRSp53 I-BAR domain induced curved membranes 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.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted February 10, 2021.
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Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53
Kaushik Inamdar, Feng-Ching Tsai, Aurore de Poret, Rayane Dibsy, John Manzi, Peggy Merida, Remi Muller, Pekka Lappalainen, Philippe Roingeard, Johnson Mak, Patricia Bassereau, Cyril Favard, Delphine Muriaux
bioRxiv 2021.02.10.430663; doi: https://doi.org/10.1101/2021.02.10.430663
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Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53
Kaushik Inamdar, Feng-Ching Tsai, Aurore de Poret, Rayane Dibsy, John Manzi, Peggy Merida, Remi Muller, Pekka Lappalainen, Philippe Roingeard, Johnson Mak, Patricia Bassereau, Cyril Favard, Delphine Muriaux
bioRxiv 2021.02.10.430663; doi: https://doi.org/10.1101/2021.02.10.430663

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