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Isolation and partial characterization of polymyxin B-resistant isolates of Vibrio parahaemolyticus

T Koga1, K Takumi

  • 1Department of Food Microbiology, Tokushima University School of Medicine, Japan.

Insights

Polymyxin-resistant Vibrio parahaemolyticus showed increased cell envelope protein content. A novel 26 K protein emerged in resistant strains, linked to polymyxin resistance and low salt conditions.

Area of Science:

  • Microbiology
  • Bacterial Physiology
  • Drug Resistance

Background:

  • Polymyxins are critical last-resort antibiotics against Gram-negative bacteria.
  • Mechanisms of polymyxin resistance in Vibrio parahaemolyticus are not fully understood.
  • Alterations in cell envelope composition are often associated with antibiotic resistance.

Purpose of the Study:

  • To investigate the cell envelope and outer membrane protein composition of polymyxin-resistant Vibrio parahaemolyticus isolates.
  • To identify potential molecular changes contributing to polymyxin resistance in this pathogen.

Main Methods:

  • Isolation and characterization of spontaneous polymyxin-resistant Vibrio parahaemolyticus strains.
  • Comparative analysis of cell envelope protein content between resistant and sensitive strains.
  • Outer membrane protein profiling using SDS-PAGE.
  • Growth studies in the presence/absence of polymyxin and varying NaCl concentrations.

Main Results:

  • Polymyxin-resistant isolates exhibited significantly higher cell envelope protein content compared to sensitive strains.
  • A novel 26,000 molecular weight (26 K) outer membrane protein was uniquely produced by resistant isolates.
  • Production of the 26 K protein was induced by polymyxin exposure and also observed under low NaCl conditions (0.2-0.5%).

Conclusions:

  • Increased cell envelope protein content and the novel 26 K protein are associated with polymyxin resistance in Vibrio parahaemolyticus.
  • The 26 K protein may play a role in polymyxin resistance, potentially influenced by environmental factors like salinity.

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