Balancing mcr-1 expression and bacterial survival is a delicate equilibrium between essential cellular defence mechanisms

Nat Commun. 2017 Dec 12;8(1):2054. doi: 10.1038/s41467-017-02149-0.

Abstract

MCR-1 is a lipid A modifying enzyme that confers resistance to the antibiotic colistin. Here, we analyse the impact of MCR-1 expression on E. coli morphology, fitness, competitiveness, immune stimulation and virulence. Increased expression of mcr-1 results in decreased growth rate, cell viability, competitive ability and significant degradation in cell membrane and cytoplasmic structures, compared to expression of catalytically inactive MCR-1 (E246A) or MCR-1 soluble component. Lipopolysaccharide (LPS) extracted from mcr-1 strains induces lower production of IL-6 and TNF, when compared to control LPS. Compared to their parent strains, high-level colistin resistance mutants (HLCRMs) show reduced fitness (relative fitness is 0.41-0.78) and highly attenuated virulence in a Galleria mellonella infection model. Furthermore, HLCRMs are more susceptible to most antibiotics than their respective parent strains. Our results show that the bacterium is challenged to find a delicate equilibrium between expression of MCR-1-mediated colistin resistance and minimalizing toxicity and thus ensuring cell survival.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Bacterial Agents / pharmacology*
  • Anti-Bacterial Agents / therapeutic use
  • Cell Membrane / pathology
  • Colistin / pharmacology
  • Colistin / therapeutic use
  • Disease Models, Animal
  • Drug Resistance, Bacterial / physiology*
  • Escherichia coli / pathogenicity
  • Escherichia coli / physiology*
  • Escherichia coli Infections / drug therapy*
  • Escherichia coli Infections / pathology
  • Escherichia coli Proteins / physiology*
  • Humans
  • Larva / microbiology
  • Microbial Sensitivity Tests
  • Moths / microbiology

Substances

  • Anti-Bacterial Agents
  • Escherichia coli Proteins
  • MCR-1 protein, E coli
  • Colistin