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Nucleocapsid Annealing-Mediated Electrophoresis NAME Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
Published on: January 19, 2015
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Quenching protein dynamics interferes with HIV capsid maturation
Mingzhang Wang1,2, Caitlin M Quinn1,2, Juan R Perilla3,4
1Department of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.
Nature Communications
|November 28, 2017
Summary
HIV-1 maturation involves Gag protein changes. We found the SP1 peptide
Area of Science:
- Structural Biology
- Virology
- Biochemistry
Background:
- HIV-1 particle maturation is a complex process involving Gag polyprotein cleavage.
- The structure of the CA-SP1 region, an intermediate during maturation, remains incompletely understood.
- Understanding CA-SP1 dynamics is crucial for developing novel HIV-1 maturation inhibitors.
Purpose of the Study:
- To elucidate the structural dynamics of the CA-SP1 intermediate during HIV-1 maturation.
- To investigate the impact of maturation inhibitors and mutations on CA-SP1 structure and dynamics.
- To explore novel therapeutic strategies targeting HIV-1 maturation.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy.
- Cryo-electron microscopy (cryo-EM).
- Molecular dynamics (MD) simulations.
Main Results:
- In vitro assembled CA-SP1 tubes reveal SP1 peptide in a dynamic helix-coil equilibrium.
- Maturation inhibitors Bevirimat and DFH-055 stabilize a helical SP1 conformation.
- The SP1 mutation T8I induces helical structure and global conformational changes in CA.
Conclusions:
- CA and SP1 dynamics are essential for ordered HIV-1 maturation.
- Small molecules can inhibit HIV-1 maturation by disrupting essential molecular motions.
- Targeting CA-SP1 dynamics offers a promising strategy for antiviral drug development.
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