Accessory mutations maintain stability in drug-resistant HIV-1 protease.

@article{Chang2011AccessoryMM,
  title={Accessory mutations maintain stability in drug-resistant HIV-1 protease.},
  author={Max W. Chang and Bruce E. Torbett},
  journal={Journal of molecular biology},
  year={2011},
  volume={410 4},
  pages={756-60}
}
The underlying mechanisms driving the evolution of drug resistance in human immunodeficiency virus (HIV) are only partially understood. We investigated the evolutionary cost of the major resistance mutations in HIV-1 protease in terms of protein stability. The accumulation of resistance mutations destabilizes the protease, limiting further adaptation. From an analysis of clinical isolates, we identified specific accessory mutations that were able to restore the stability of the protease or even… CONTINUE READING

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