Yersinia pseudotuberculosis and Yersinia pestis are more resistant to bactericidal cationic peptides than Yersinia enterocolitica
Open Access
- 1 June 1998
- journal article
- research article
- Published by Microbiology Society in Microbiology
- Vol. 144 (6), 1509-1515
- https://doi.org/10.1099/00221287-144-6-1509
Abstract
The action of bactericidal polycationic peptides was compared in Yersinia spp. by testing peptide binding to live cells and changes in outer membrane (OM) morphology and permeability. Moreover, polycation interaction with LPS was studied by measuring the dependence of dansylcadaverine displacement and zeta potential on polycation concentration. When grown at 37 °C, Yersinia pestis and Yersinia pseudotuberculosis bound less polymyxin B (PMB) than pathogenic or non-pathogenic Yersinia enterocolitica, regardless of virulence plasmid expression. Y. pseudotuberculosis OMs were unharmed by PMB concentrations causing extensive OM blebbing in Y. enterocolitica. The permeability to Iysozyme caused by PMB was greater in Y. enterocolitica than in Y. pseudotuberculosis or Y. pestis and differences increased at 37 °C. Similar observations were made with other polycations using a polymyxin/novobiocin permeability assay. With LPS of cells grown at 26 °C, polycation binding was highest for Y. pseudotuberculosis and lowest for Y. pestis, with Y. enterocolitica yielding intermediate results which were lower for pathogenic than for non-pathogenic strains. With LPS of cells grown at 37 °C, polycation binding remained unchanged for Y. pastis and pathogenic Y. enterocolitica, increased for non-pathogenic Y. enterocolitica and decreased for Y. pseudotuberculosis to Y. pestis levels. Polycation binding related in part to differences in charge density (zeta potential) of LPS aggregates, suggesting similar effects at bacterial surfaces. It is suggested that species and temperature differences in polycation resistance relate to infection route, invasiveness and intracellular multiplication of Yersinia spp.Keywords
This publication has 18 references indexed in Scilit:
- Yersinia pseudotuberculosis and Yersinia pestis show increased outer membrane permeability to hydrophobic agents which correlates with lipopolysaccharide acyl-chain fluidityMicrobiology, 1998
- Regulation of Lipid A Modifications by Salmonella typhimurium Virulence Genes phoP-phoQScience, 1997
- Characterization of Lipopolysaccharides of Polymyxin‐Resistant and Polymyxin‐Sensitive Klebsiella pneumoniae O3European Journal of Biochemistry, 1996
- PEPTIDES AS WEAPONS AGAINST MICROORGANISMS IN THE CHEMICAL DEFENSE SYSTEM OF VERTEBRATESAnnual Review of Microbiology, 1995
- Environmental Control of Virulence Functions and Signal Transduction in Yersinia EnterocoliticaPublished by Springer Science and Business Media LLC ,1995
- How bacteria resist killing by host-defense peptidesTrends in Microbiology, 1994
- Increased substitution of phosphate groups in lipopolysaccharides and lipid A of the polymyxin‐resistant pmrA mutants of Salmonella typhimurium: a 31P‐NMR studyMolecular Microbiology, 1994
- Analysis of the binding of polymyxin B to endotoxic lipid A and core glycolipid using a fluorescent displacement probeBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1992
- Factors promoting acute and chronic diseases caused by yersiniaeClinical Microbiology Reviews, 1991
- [16] Measuring electrostatic potentials adjacent to membranesMethods in enzymology, 1989