AI Article Synopsis
- The study demonstrates that the I-BAR protein IRSp53 is essential for HIV-1 particle formation by aiding the necessary membrane curvature alongside the Gag protein.
- When IRSp53 is knocked down using siRNA, there’s a notable reduction in the production of viral particles, leading to incomplete assembly during the budding process.
- The research highlights a direct interaction between IRSp53 and Gag at the plasma membrane, suggesting that IRSp53 not only supports membrane curvature but is also found in the structure of the HIV-1 particles.
Article 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.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8260224 | PMC |
| http://dx.doi.org/10.7554/eLife.67321 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!