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Related Experiment Video

Updated: Jun 9, 2026

Rapid Screening of HIV Reverse Transcriptase and Integrase Inhibitors

Rapid Screening of HIV Reverse Transcriptase and Integrase Inhibitors

Published on: April 9, 2014

An Inducible ESCRT-III Inhibition Tool to Control HIV-1 Budding.

Haiyan Wang¹, Benoit Gallet¹, Christine Moriscot²

¹University Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 38000 Grenoble, France.

|December 23, 2023

Summary

Researchers developed a drug-inducible tool to study the Endosomal Sorting Complex Required for Transport (ESCRT)-III machinery during HIV-1 budding. This tool enhances ESCRT-III lifetime, revealing its critical role in viral release and offering new insights into cellular processes.

Keywords:

CHMP2A CHMP3 CHMP4B ESCRT-III HIV-1 VLP release modulation budding membrane fission membrane remodeling

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Area of Science:

Cell Biology
Virology
Molecular Medicine

Background:

The Endosomal Sorting Complex Required for Transport (ESCRT) machinery is essential for HIV-1 budding and other cellular functions.
Limited understanding of ESCRT-III complex architecture at HIV-1 budding sites due to spatial resolution and transient recruitment.

Purpose of the Study:

To develop a drug-inducible tool to stabilize ESCRT-III at HIV-1 budding sites, enhancing its lifetime.
To investigate the functional consequences of inhibiting ESCRT-III during HIV-1 budding.

Main Methods:

Generated autocleavable CHMP2A, CHMP3, and CHMP4B fusion proteins with hepatitis C virus NS3 protease.
Characterized fusion proteins' expression, stability, localization, and effect on HIV-1 Gag VLP budding in the presence/absence of protease inhibitor Glecaprevir.
Utilized immunoblotting, localization studies, transmission electron microscopy, and video-microscopy.

Main Results:

CHMP-NS3 fusion proteins showed rapid and stable accumulation.
Drug administration led to CHMP2A-NS3 and CHMP4B-NS3 fusion proteins decreasing VLP release, while CHMP3-NS3 showed no effect but synergized with CHMP2A-NS3.
Fusion proteins relocalized to plasma membrane, endosomes, and budding sites, causing drug-dependent accumulation and delayed HIV-1 Gag-VLP release.

Conclusions:

Novel insights into ESCRT-III inhibition during HIV-1 budding.
Established new tools for deciphering ESCRT-III roles in HIV-1 budding and other ESCRT-catalyzed cellular processes.