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Interaction between human immunodeficiency virus type 1 reverse transcriptase and integrase proteins.

Eric A Hehl1, Pheroze Joshi, Ganjam V Kalpana

  • 1Department of Microbiology and Immunology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.

Journal of Virology
|April 29, 2004
PubMed
Summary

Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) and integrase (IN) interact, with RT stimulating IN

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Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Retroviruses encode two key enzymes: reverse transcriptase (RT) and integrase (IN).
  • Previous studies indicated a specific interaction between HIV-1 RT and IN proteins.
  • Understanding this interaction is crucial for deciphering viral replication mechanisms.

Purpose of the Study:

  • To map the binding domains between HIV-1 RT and IN.
  • To determine the functional consequences of the RT-IN interaction on enzyme activity.
  • To investigate the role of IN oligomerization in RT binding.

Main Methods:

  • Utilized recombinant purified HIV-1 RT and IN proteins, including mutants.
  • Employed binding assays to identify interacting domains on both enzymes.

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  • Assessed enzyme activities (RT processivity, IN 3' processing and strand transfer) in the presence of both proteins.
  • Used micrococcal nuclease treatment to rule out nucleic acid bridging.

    • Main Results:

    • HIV-1 RT (heterodimer, p66, p51) binds to HIV-1 IN.
    • The C-terminal domain of IN interacts with RT's fingers-palm and connection subdomain.
    • RT stimulates IN-mediated strand transfer up to 155-fold, while IN does not affect RT processivity.
    • IN oligomerization is not required for RT interaction.

    Conclusions:

    • Identified specific binding domains for HIV-1 RT and IN interaction.
    • Demonstrated a functional consequence: RT significantly enhances IN strand transfer activity.
    • These findings suggest a cooperative functional interaction between RT and IN during HIV-1 replication.