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Related Concept Videos

Inhibitors of Viral Protein Synthesis01:30

Inhibitors of Viral Protein Synthesis

Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...
Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...

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Related Experiment Video

Updated: Jun 15, 2026

Nucleocapsid Annealing-Mediated Electrophoresis NAME Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
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Structural Basis for HIV-1 Maturation Inhibition by PF-46396 Determined by MAS NMR.

Roman Zadorozhnyi, Caitlin M Quinn, Kaneil K Zadrozny

    Biorxiv : the Preprint Server for Biology
    |August 12, 2025
    PubMed
    Summary
    This summary is machine-generated.

    This study reveals the atomic structure of HIV-1 maturation inhibitor PF-46396 bound to capsid protein assemblies. The findings explain how PF-46396 works and offer insights into potential drug resistance mechanisms.

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    Area of Science:

    • Structural Biology
    • Virology
    • Medicinal Chemistry

    Background:

    • HIV-1 maturation inhibitors targeting the Gag lattice are crucial for antiretroviral therapy.
    • Stabilizing the capsid protein C-terminal domain (CA CTD) and spacer peptide 1 (SP1) junction is a key mechanism.

    Purpose of the Study:

    • To determine the atomic-resolution structure of CA CTD-SP1 assemblies with PF-46396 and inositol hexakisphosphate (IP6).
    • To elucidate the binding modes of PF-46396 enantiomers and their effect on IP6 dynamics.
    • To establish the structural basis for PF-46396's anti-HIV activity and drug resistance.

    Main Methods:

    • Magic Angle Spinning (MAS) Nuclear Magnetic Resonance (NMR) spectroscopy was used.
    • Atomic-resolution structural determination of protein-inhibitor-cofactor complexes.

    Main Results:

    • Distinct binding modes were observed for the two PF-46396 enantiomers, yet both showed similar anti-HIV potency.
    • PF-46396 binding arrested inositol hexakisphosphate (IP6) dynamics within the six-helix bundle pore.
    • Unique IP6 orientations were induced by each enantiomer, suggesting the presence of a monoanionic IP6 form.

    Conclusions:

    • The study provides the structural foundation for understanding PF-46396's mechanism of action as an HIV-1 maturation inhibitor.
    • A mechanistic model for drug resistance associated with PF-46396 is proposed.
    • Insights into the role of IP6 in the Gag lattice and inhibitor binding are presented.