The role of polymorphisms at position 89 in the HIV-1 protease gene in the development of drug resistance to HIV-1 protease inhibitors

J Antimicrob Chemother. 2012 Apr;67(4):988-94. doi: 10.1093/jac/dkr582. Epub 2012 Feb 7.

Abstract

Objectives: Relatively little is known about the development of resistance to protease inhibitors (PIs) in non-B subtypes. In subtype B viruses, L89 is commonly found at position 89 in the HIV protease (PR) gene, whereas M89 is commonly observed as a polymorphism in other subtypes. We compared the frequencies of substitutions at position 89 in PR in tissue culture selections and in clinical databases of PI-naive and PI-experienced populations.

Methods: Representative subtype A/CRF01_AE (n = 2 and 3) and subtype C (n = 5) isolates were cultured in MT-2 cells and cord blood mononuclear cells (CBMCs), respectively, under increasing drug pressure with PIs, and drug resistance mutations were identified.

Results: The M89 natural polymorphism in non-B subtypes commonly led to the appearance of an M89T mutation in selections with atazanavir in subtypes A/AE and C, and was accompanied by other previously recognized atazanavir mutations. The M89T mutation contributed to phenotypic resistance to atazanavir and cross-resistance to lopinavir and nelfinavir, but not to other PIs. A shift from a L89 natural polymorphism to L89I/M arose in two of five subtype C selections with PIs. M89I/V/T mutations were acquired by 10%-11% of individuals harbouring non-B subtypes who were failing PI-based regimens, but were rarely observed in drug-naive persons and in patients failing non-PI-based regimens.

Conclusions: The M/L89 natural polymorphism present in non-B subtypes may lead to the M89T mutational pathway conferring resistance to atazanavir, lopinavir and nelfinavir.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Anti-HIV Agents / pharmacology*
  • Atazanavir Sulfate
  • Cells, Cultured
  • Drug Resistance, Viral*
  • Genotype
  • HIV Infections / virology*
  • HIV Protease / genetics*
  • HIV Protease Inhibitors / pharmacology*
  • HIV-1 / classification
  • HIV-1 / genetics*
  • HIV-1 / isolation & purification
  • Humans
  • Leukocytes, Mononuclear / virology
  • Lopinavir / pharmacology
  • Nelfinavir / pharmacology
  • Oligopeptides / pharmacology
  • Polymorphism, Genetic*
  • Pyridines / pharmacology
  • Virus Cultivation

Substances

  • Anti-HIV Agents
  • HIV Protease Inhibitors
  • Oligopeptides
  • Pyridines
  • Lopinavir
  • Atazanavir Sulfate
  • HIV Protease
  • p16 protease, Human immunodeficiency virus 1
  • Nelfinavir