Journal of Antimicrobial Chemotherapy, Vol 40, 615-621, Copyright © 1997 by The British Society for Antimicrobial Chemotherapy
JL Kadurugamuwa and TJ Beveridge
Pseudomonas aeruginosa (and various other gram-negative pathogens) liberate
membrane vesicles during normal growth. These bilayered vesicles consist of
endotoxin (lipopolysaccharide), outer membrane proteins and several potent
hydrolytic enzymes including protease, alkaline phosphatase, phospholipase
C and peptidoglycan hydrolase. The vesicles contain pro-elastase and
alkaline phosphatase (which are periplasmic constituents) and so are
important for packaging periplasmic components as they are liberated to the
outside of the cell. Once liberated, the vesicles are capable of fusing
with the membranes of epithelial cells and liberating their virulence
factors into host cells where they degrade cellular components, thereby
aiding infection by the pathogen. The aminoglycoside antibiotic,
gentamicin, is thought to kill bacteria by inhibiting protein synthesis,
yet this cationic antibiotic can also perturb the packing order of lipids,
thereby destabilizing bilayered membranes. For pathogens with highly
anionic lipopolysaccharide on their surface, such as P. aeruginosa, this
membrane destabilization can be so serious that it can cause cell lysis;
these cells are therefore killed by a combination of protein synthesis
inhibition and surface perturbation. By destabilizing the membranes of P.
aeruginosa, gentamicin increases the release of membrane vesicles three- to
five-fold. This may help account for some of the bacterium-mediated
toxicity encountered during patient treatment with aminoglycoside
antibiotics.
REVIEWS
Natural release of virulence factors in membrane vesicles by Pseudomonas aeruginosa and the effect of aminoglycoside antibiotics on their release
Department of Microbiology, College of Biological Science, University of Guelph, Ontario, Canada.
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