Premium
Temperature‐regulated efflux pump/potassium antiporter system mediates resistance to cationic antimicrobial peptides in Yersinia
Author(s) -
Bengoechea José Antonio,
Skurnik Mikael
Publication year - 2000
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2000.01956.x
Subject(s) - antiporter , efflux , biology , polymyxin , microbiology and biotechnology , bacteria , polymyxin b , antimicrobial peptides , transmembrane protein , antimicrobial , bacterial outer membrane , lipopolysaccharide , biochemistry , escherichia coli , membrane , antibiotics , gene , genetics , immunology , receptor
Most bacterial pathogens are resistant to cationic antimicrobial peptides (CAMPs) that are key components of the innate immunity of both vertebrates and invertebrates. In Gram‐negative bacteria, the known CAMPs resistance mechanisms involve outer membrane (OM) modifications and specifically those in the lipopolysaccharide (LPS) molecule. Here we report, the characterization of a novel CAMPs resistance mechanism present in Yersinia that is dependent on an efflux pump/potassium antiporter system formed by the RosA and RosB proteins. The RosA/RosB system is activated by a temperature shift to 37°C, but is also induced by the presence of the CAMPs, such as polymyxin B. This is the first report of a CAMPs resistance system that is induced by the presence of CAMPs. It is proposed that the RosA/RosB system protects the bacteria by both acidifying the cytoplasm to prevent the CAMPs action and pumping the CAMPs out of the cell.