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Deciphering MCR-2 Colistin Resistance.

Jian Sun1,2, Yongchang Xu1, Rongsui Gao1

  • 1Department of Medical Microbiology and Parasitology, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.

Mbio
|May 11, 2017
PubMed
Summary
This summary is machine-generated.

The newly discovered mcr-2 gene facilitates colistin resistance in bacteria through a unique transposon. Understanding its molecular mechanisms and origin is crucial for combating multidrug-resistant pathogens.

Keywords:
MCR-1MCR-2colistin resistancedisseminationdomain swappingoriginplasmid transferstructure-guided mutagenesis

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Genetics

Background:

  • Antibiotic resistance, particularly to carbapenems and colistin, is a critical global health challenge.
  • Colistin is a last-resort antibiotic against multidrug-resistant Gram-negative infections.
  • The emergence of plasmid-borne colistin resistance genes, like mcr-1 and the newly identified mcr-2, threatens treatment options.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying mcr-2-mediated colistin resistance.
  • To investigate the origin and transfer mechanisms of the mcr-2 gene.
  • To identify key functional domains and motifs within the MCR-2 protein.

Main Methods:

  • Evolutionary analysis to trace the origin of mcr-2.
  • Transcriptional analysis to compare mcr-2 and mcr-1 expression levels.
  • Genetic deletions and domain swapping to assess the role of transmembrane regions (TM1, TM2).
  • MALDI-TOF MS to confirm MCR protein activity on lipopolysaccharide (LPS).
  • Site-directed mutagenesis to define the catalytic motif.

Main Results:

  • A unique transposon unit facilitates the acquisition and transfer of mcr-2.
  • mcr-2 and mcr-1 likely originated from a phosphoethanolamine (PEA) lipid A transferase in *Paenibacillus*.
  • mcr-2 exhibits higher transcript levels compared to mcr-1.
  • Transmembrane regions TM1 and TM2 are essential for MCR-1/MCR-2 localization and function, with TM2 being more efficient.
  • MCR proteins catalyze the addition of PEA to LPS, conferring colistin resistance.
  • A 6-residue zinc-binding/catalytic motif is essential for MCR-2 function.

Conclusions:

  • The study provides mechanistic insights into transferable colistin resistance mediated by mcr-2.
  • The findings highlight the role of a unique transposon in mcr-2 dissemination.
  • Understanding MCR-2's periplasmic localization and catalytic activity is key to developing targeted therapeutics.
  • Identification of the essential catalytic motif offers potential targets for combating mcr-2-mediated resistance.