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HIV-1 protease activation relies on Gag-Pol dimerization, which is modulated by reverse transcriptase (RT) interactions. Targeting RT/RT interactions could offer a novel anti-HIV therapy by inhibiting both RT and protease activity.

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Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Proteolytic processing by human immunodeficiency virus type 1 protease (PR) is crucial for viral infectivity.
  • PR activation is triggered by Gag-Pol dimerization during virus assembly.
  • Previous studies linked reverse transcriptase (RT) mutations to altered PR activity and efavirenz (EFV) response.

Purpose of the Study:

  • To investigate the role of the RT domain in modulating PR activation through Gag-Pol dimerization.
  • To explore the involvement of a leucine repeat motif (LRM) in RT/RT interactions.

Main Methods:

  • Amino acid substitutions in the RT LRM and a dimerization-defective mutant (W401A) were created.
  • Gag cleavage efficiency was assessed in the presence and absence of EFV.
  • Leucine zipper (LZ) motifs were used to probe Gag-Pol dimerization dynamics.

Main Results:

  • LRM mutations destabilized RT and reduced PR-mediated Gag cleavage, attenuating EFV's enhancement effect.
  • The W401A mutant and LZ insertion impaired Gag cleavage, indicating disruption of Gag-Pol dimerization.
  • Combined EFV and W402A treatment markedly impaired Gag cleavage, suggesting EFV disrupts W402A Gag-Pol dimerization.

Conclusions:

  • RT modulates PR activation by influencing Gag-Pol/Gag-Pol interactions.
  • RT/RT interaction is critical for triggering PR activation via Gag-Pol dimerization.
  • Targeting RT/RT interactions presents a potential therapeutic strategy for HIV-1 by inhibiting both PR and RT activity.