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Non-nucleoside Reverse Transcriptase Inhibitors Inhibit Reverse Transcriptase through a Mutually Exclusive

Jeffrey J DeStefano1

  • 1Department of Cell Biology and Molecular Genetics and the Maryland Pathogen Research Institute , University of Maryland , College Park , Maryland 20742 , United States.

Biochemistry
|March 23, 2019
PubMed
Summary

Non-nucleoside reverse transcriptase inhibitors (NNRTIs) and divalent cation-dNTP complexes mutually inhibit each other

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Virology

Background:

  • Non-nucleoside reverse transcriptase inhibitors (NNRTIs) are crucial in HIV treatment, acting as noncompetitive inhibitors of reverse transcriptase (RT).
  • Understanding the precise binding interactions between NNRTIs, divalent cations, dNTPs, and RT is essential for developing more effective antiviral therapies.
  • Previous studies have suggested various mechanisms of NNRTI inhibition, but the competitive or mutually exclusive nature of binding with essential cofactors remains an area of active investigation.

Purpose of the Study:

  • To biochemically investigate the binding interactions between NNRTIs, divalent cations, and dNTPs with reverse transcriptase (RT) in the presence of primer/template (P/T) complexes.
  • To determine the relative binding affinities of different divalent cations (Mg2+, Mn2+, Zn2+, Co2+, Ni2+) with dNTPs to RT-P/T complexes.
  • To elucidate the mechanism of inhibition, specifically whether NNRTIs and divalent cation-dNTP complexes compete for binding to RT-P/T.

Main Methods:

  • Biochemical assays including filtration and primer extension assays were employed.
  • The binding of various divalent cation-dNTP complexes (using Mg2+, Mn2+, Zn2+, Co2+, Ni2+) to RT-P/T complexes was measured, with Ca2+ used as a noncatalytic control.
  • The inhibitory effects of NNRTIs (efavirenz, rilpivirine, nevirapine) on dNTP binding and the inhibitory effects of divalent cation-dNTP complexes on NNRTI binding were quantified.

Main Results:

  • Divalent cation-dNTP complexes exhibited varying binding strengths to RT-P/T, with Mn2+ and Zn2+ showing the strongest affinity.
  • NNRTIs and divalent cation-dNTP complexes demonstrated mutually exclusive binding, with stronger cation-dNTP complexes conferring greater resistance to NNRTI inhibition.
  • Efavirenz (EFV) binding to wild-type and K103N mutant RT-P/T complexes was inhibited by divalent cation-dNTP complexes, with Mn2+-dNTP complexes being more potent inhibitors than Mg2+-dNTP complexes.

Conclusions:

  • The study provides strong biochemical evidence supporting mutually exclusive binding between NNRTIs and divalent cation-dNTP complexes to RT-P/T.
  • The binding affinity of divalent cations significantly influences the resistance of RT to NNRTI inhibition.
  • The findings offer insights into the resistance mechanisms associated with NNRTI-resistant RT mutations, such as K103N, suggesting weaker drug binding as a primary factor.