Exploiting evolutionary trade-offs for posttreatment management of drug-resistant populations

Proc Natl Acad Sci U S A. 2020 Jul 28;117(30):17924-17931. doi: 10.1073/pnas.2003132117. Epub 2020 Jul 13.

Abstract

Antibiotic resistance frequently evolves through fitness trade-offs in which the genetic alterations that confer resistance to a drug can also cause growth defects in resistant cells. Here, through experimental evolution in a microfluidics-based turbidostat, we demonstrate that antibiotic-resistant cells can be efficiently inhibited by amplifying the fitness costs associated with drug-resistance evolution. Using tavaborole-resistant Escherichia coli as a model, we show that genetic mutations in leucyl-tRNA synthetase (that underlie tavaborole resistance) make resistant cells intolerant to norvaline, a chemical analog of leucine that is mistakenly used by tavaborole-resistant cells for protein synthesis. We then show that tavaborole-sensitive cells quickly outcompete tavaborole-resistant cells in the presence of norvaline due to the amplified cost of the molecular defect of tavaborole resistance. This finding illustrates that understanding molecular mechanisms of drug resistance allows us to effectively amplify even small evolutionary vulnerabilities of resistant cells to potentially enhance or enable adaptive therapies by accelerating posttreatment competition between resistant and susceptible cells.

Keywords: adaptive therapy; evolutionary trade-offs; mistranslation; protein synthesis; therapeutic resistance.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Biological Evolution*
  • Drug Resistance*
  • Drug Resistance, Bacterial
  • Escherichia coli / drug effects
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics
  • Genetic Variation
  • Models, Molecular
  • Protein Conformation
  • Structure-Activity Relationship

Substances

  • Anti-Bacterial Agents
  • Escherichia coli Proteins

Associated data

  • figshare/10.6084/m9.figshare.11886288.v2