Understanding the structural mechanisms of antibiotic resistance sets the platform for new discovery

Future Microbiol. 2015;10(11):1727-33. doi: 10.2217/fmb.15.78. Epub 2015 Oct 30.

Abstract

Understanding the structural basis of antibacterial resistance may enable rational design principles that avoid and subvert that resistance, thus leading to the discovery of more effective antibiotics. In this review, we explore the use of crystal structures to guide new discovery of antibiotics that are effective against resistant organisms. Structures of efflux pumps bound to substrates and inhibitors have aided the design of compounds with lower affinity for the pump or inhibitors that more effectively block the pump. Structures of β-lactamase enzymes have revealed the mechanisms of action toward key carbapenems and structures of gyrase have aided the design of compounds that are less susceptible to point mutations.

Keywords: crystal structures; efflux pump; gyrase; β-lactamase.

Publication types

  • Review

MeSH terms

  • Anti-Bacterial Agents / isolation & purification
  • Anti-Bacterial Agents / pharmacology*
  • Bacteria / drug effects*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Crystallography, X-Ray
  • Drug Discovery / methods*
  • Drug Resistance, Bacterial*
  • Humans
  • Molecular Docking Simulation
  • Protein Conformation

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins