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Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
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CPSF6 defines a conserved capsid interface that modulates HIV-1 replication.

Amanda J Price1, Adam J Fletcher, Torsten Schaller

  • 1Medical Research Council Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Cambridge, United Kingdom.

Plos Pathogens
|September 8, 2012
PubMed
Summary
This summary is machine-generated.

A newly discovered protein interface on the HIV-1 capsid (CA) protein is crucial for viral infection. This interface interacts with host factors, influencing viral restriction and cofactor dependence.

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • The human immunodeficiency virus type 1 (HIV-1) genome is protected by a capsid (CA) protein shell during cell entry.
  • CA sequence variations impact HIV-1 infectivity and evasion of host defenses.
  • Previously, only the Cyclophilin A-binding loop was known as a CA interaction site for cellular cofactors.

Purpose of the Study:

  • To identify and characterize novel protein-protein interfaces on the HIV-1 CA N-terminal domain.
  • To elucidate the role of these interfaces in mediating viral restriction and host cofactor interactions.
  • To understand how these interactions influence HIV-1 infectivity and nuclear import.

Main Methods:

  • X-ray crystallography was employed to determine the structure of the novel CA protein-protein interface.
  • Site-directed mutagenesis was used to create mutations in the identified interface.
  • Binding assays were performed to assess the interaction of mutated CA with CPSF6-358.
  • Functional assays were conducted to evaluate the impact of mutations on cofactor dependence (TNPO3, RanBP2) and viral infectivity.

Main Results:

  • A novel, highly conserved protein-protein interface was identified in the N-terminal domain of HIV-1 CA, accessible within a hexameric lattice.
  • Mutations disrupting this interface abolished binding to CPSF6-358 (a fragment of cleavage and polyadenylation specific factor 6).
  • Disruption of the interface also abrogated the dependence on nuclear entry cofactors TNPO3 and RanBP2.
  • These findings indicate that the HIV-1 capsid directly engages host cofactors.

Conclusions:

  • The HIV-1 capsid possesses a novel interface that directly mediates interactions with host cellular cofactors.
  • This interface plays a critical role in viral restriction and is essential for dependence on specific host cofactors like CPSF6, TNPO3, and RanBP2.
  • Understanding this capsid-cofactor interaction provides new insights into HIV-1 infection mechanisms and potential therapeutic targets.