Molecular Microbiology · 2010 · 32 citations · 55 references
Life SciencesMicrobiologyMolecular BiologyAntimicrobial ResistanceBacteriologyMicrobial PathogenesisAntibacterial ResistanceAntibiotic ResistanceBacterial Secretion SystemsPulmonary InfectionsQuorum SensingCellular Membrane PermeabilizationDegradationFlagellar Virulence FactorsLysozyme ActivityMembrane PermeabilizationOuter Membrane ProteinsPseudomonas Aeruginosa ResistanceSurfactant Protein Deficiency
Surfactant protein-A (SP-A) is an important antimicrobial protein that opsonizes and permeabilizes membranes of microbial pathogens in mammalian lungs. Previously, we have shown that Pseudomonas aeruginosa flagellum-deficient mutants are preferentially cleared in the lungs of wild-type mice by SP-A-mediated membrane permeabilization, and not by opsonization. In this study, we report a flagellum-mediated mechanism of P. aeruginosa resistance to SP-A. We discovered that flagellum-deficient (ΔfliC) bacteria are unable to produce adequate amounts of exoproteases to degrade SP-A in vitro and in vivo, leading to its preferential clearance in the lungs of SP-A(+/+) mice. In addition, ΔfliC bacteria failed to degrade another important lung antimicrobial protein lysozyme. Detailed analyses showed that ΔfliC bacteria are unable to upregulate the transcription of lasI and rhlI genes, impairing the production of homoserine lactones necessary for quorum-sensing, an important virulence process that regulates the production of multiple exoproteases. Thus, reduced ability of ΔfliC bacteria to quorum-sense attenuates production of exoproteases and limits degradation of SP-A, thereby conferring susceptibility to this major pulmonary host defence protein.
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Molecular cloning: A laboratory manual
Prescott L. Deininger · Analytical Biochemistry · 1990 · 86.2K citations
Regulation of las and rhl quorum sensing in Pseudomonas aeruginosa
Everett C. Pesci, James P. Pearson, Patrick C. Seed et al. · Journal of Bacteriology · 1997 · 906 citations · Full text