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Isolation and Chemical Characterization of Lipid A from Gram-negative Bacteria
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Isolation and Chemical Characterization of Lipid A from Gram-negative Bacteria

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Comparative analysis of phosphoethanolamine transferases involved in polymyxin resistance across 10 clinically

Jiayuan Huang1, Yan Zhu1, Mei-Ling Han2

  • 1Infection and Immunity Programme, Monash Biomedicine Discovery Institute, Monash University, Victoria, Australia; Department of Microbiology, Monash University, Victoria, Australia.

International Journal of Antimicrobial Agents
|December 31, 2017
PubMed

Insights

Gram-negative superbugs threaten global health, leading to polymyxin resistance. This study analyzes phosphoethanolamine (PEA) transferases, revealing conserved functional sites crucial for understanding resistance mechanisms.

Area of Science:

  • Microbiology
  • Genetics
  • Bioinformatics

Background:

  • Gram-negative 'superbugs' pose a significant global health threat, necessitating last-line therapies like polymyxins.
  • Polymyxin resistance arises from phosphoethanolamine (PEA) modification of lipid A, disrupting drug binding.
  • Both chromosomal and plasmid-encoded PEA transferases exist, but their diversity and function are not fully understood.

Purpose of the Study:

  • To comparatively analyze the sequence and functional heterogeneity of PEA transferases across 10 clinically relevant Gram-negative bacterial species.
  • To elucidate the evolutionary relationships between chromosomal (EptA, EptB, EptC) and plasmid-encoded (MCR-1, MCR-2) PEA transferases.
  • To identify conserved functional domains and sites within PEA transferases important for polymyxin resistance.

Main Methods:

  • Multiple sequence alignment of PEA transferase genes from representative strains of 10 bacterial species.
  • Phylogenetic analysis to evaluate evolutionary relationships and conservation patterns.
  • Comparative analysis focusing on catalytic and transmembrane domains, including PEA acceptor sites and zinc-binding pockets.

Main Results:

  • Low pairwise identity among EptA, EptB, and EptC from Escherichia coli; EptA shows highest similarity to MCR-1 and MCR-2.
  • The catalytic domain of PEA transferases is more conserved across species than the transmembrane domain.
  • High conservation of PEA acceptor sites and zinc-binding pockets suggests functional importance.
  • Intraspecies conservation of EptA is high, while interspecies conservation is low.

Conclusions:

  • Comparative analysis of PEA transferases provides critical bioinformatic insights into polymyxin resistance mechanisms.
  • Conserved functional domains and sites highlight key areas for future research into combating Gram-negative superbugs.
  • Understanding PEA transferase heterogeneity is essential for developing strategies against polymyxin-resistant bacteria.
Keywords:
Multi-drug resistanceMultiple sequence alignmentPhosphoethanolamine transferasePhylogenetic analysisPolymyxin resistance

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