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Updated: Oct 30, 2025
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Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle GUV Membranes
Published on: July 28, 2016
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Novel Tsg101 Binding Partners Regulate Viral L Domain Trafficking
Madeleine Strickland1, David Nyenhuis1, Susan M Watanabe2
1Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Viruses
|July 2, 2021
Summary
Tsg101, a key factor in HIV-1 budding, interacts with ubiquitin and tRNA. New small molecules targeting these interactions may offer antiviral drug design opportunities.
Area of Science:
- Virology
- Molecular Biology
- Structural Biology
Background:
- Tsg101, an ESCRT-I component, is recruited by HIV-1 Gag for viral budding.
- The Tsg101 N-terminal domain binds the Gag P(T/S)AP motif and ubiquitin (Ub).
- Ubiquitin binding was hypothesized to enhance P(T/S)AP interaction.
Purpose of the Study:
- To investigate novel binding partners of Tsg101.
- To explore the role of these interactions in HIV-1 assembly.
- To identify potential antiviral drug targets.
Main Methods:
- Biochemical assays to study Tsg101 interactions.
- Structural analysis of Tsg101 binding pockets.
- Small molecule screening for inhibitors.
Main Results:
- Tsg101 binds Lys63-linked di-ubiquitin with high affinity.
- Small molecules disrupting Ub binding inhibit viral budding.
- tRNA identified as a novel Tsg101 binding partner.
Conclusions:
- Tsg101 interacts with ubiquitin and tRNA, influencing HIV-1 assembly.
- These interactions present new avenues for antiviral drug development.
- Understanding Tsg101's diverse binding partners is crucial for controlling viral replication.
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