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Viral genomes exhibit remarkable diversity in size, structure, and composition, influencing their replication strategies and interactions with host cells. These genomes consist of either DNA or RNA and may be linear or circular. Additionally, they can be single-stranded or double-stranded, with each configuration affecting how the virus propagates within a host. RNA viruses, for instance, generally have smaller genomes than DNA viruses, a factor that contributes to their high mutation rates and...
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Structural basis for HIV-1 capsid adaption to a deficiency in IP6 packaging.

Yanan Zhu1,2, Alex B Kleinpeter3, Juan S Rey4

  • 1Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.

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|September 1, 2025
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A new mutation (G225R) in HIV-1 capsid protein restores infectivity in IP6-deficient viruses by stabilizing Gag lattices. This finding reveals a key role for the capsid C-terminus in viral assembly and adaptation.

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Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Inositol hexakisphosphate (IP6) is crucial for HIV-1 assembly and maturation.
  • IP6 stabilizes the Gag lattice and is essential for mature capsid formation within virions.
  • Previous studies identified Gag mutants with low IP6 packaging, leading to non-infectious particles with defective capsids.

Purpose of the Study:

  • To investigate compensatory mechanisms in HIV-1 assembly under IP6-deficient conditions.
  • To characterize a mutation in the capsid protein (CA) that restores infectivity in IP6-deficient HIV-1 mutants.
  • To elucidate the structural and functional role of the CA C-terminus in viral assembly.

Main Methods:

  • Genetic analysis of HIV-1 Gag mutants.
  • In vitro assembly assays of capsid protein (CA).
  • Cryo-electron microscopy (CryoEM) for structural determination.
  • Molecular dynamics (MD) simulations.

Main Results:

  • A compensatory mutation, G225R, in the CA C-terminus restores capsid assembly and infectivity in IP6-deficient HIV-1 mutants.
  • G225R enhances in vitro CA assembly at significantly lower IP6 concentrations compared to wild-type CA.
  • CryoEM structures reveal that G225R induces a structured CA C-terminus, stabilizing hexamer-hexamer interfaces.
  • MD simulations support the stabilizing mechanism of the G225R mutation.

Conclusions:

  • HIV-1 can adapt to IP6 deficiency through mutations like G225R in the capsid protein.
  • The CA C-terminus plays a critical, previously unrecognized structural role in stabilizing HIV-1 capsid assembly.
  • The findings provide insights into viral adaptation and offer tools for studying HIV-1 capsid formation.