Unknown

Dataset Information

0

The LasB Elastase of Pseudomonas aeruginosa Acts in Concert with Alkaline Protease AprA To Prevent Flagellin-Mediated Immune Recognition.

ABSTRACT: The opportunistic pathogen Pseudomonas aeruginosa is capable of establishing severe and persistent infections in various eukaryotic hosts. It encodes a wide array of virulence factors and employs several strategies to evade immune detection. In the present study, we screened the Harvard Medical School transposon mutant library of P. aeruginosa PA14 for bacterial factors that modulate interleukin-8 responses in A549 human airway epithelial cells. We found that in addition to the previously identified alkaline protease AprA, the elastase LasB is capable of degrading exogenous flagellin under calcium-replete conditions and prevents flagellin-mediated immune recognition. Our results indicate that the production of two proteases with anti-flagellin activity provides a failsafe mechanism for P. aeruginosa to ensure the maintenance of protease-dependent immune-modulating functions.

SUBMITTER: Casilag F 

PROVIDER: S-EPMC4693985 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

The LasB Elastase of Pseudomonas aeruginosa Acts in Concert with Alkaline Protease AprA To Prevent Flagellin-Mediated Immune Recognition.

Casilag Fiordiligie F   Lorenz Anne A   Krueger Jonas J   Klawonn Frank F   Weiss Siegfried S   Häussler Susanne S  

Infection and immunity 20151026 1

The opportunistic pathogen Pseudomonas aeruginosa is capable of establishing severe and persistent infections in various eukaryotic hosts. It encodes a wide array of virulence factors and employs several strategies to evade immune detection. In the present study, we screened the Harvard Medical School transposon mutant library of P. aeruginosa PA14 for bacterial factors that modulate interleukin-8 responses in A549 human airway epithelial cells. We found that in addition to the previously identi  ...[more]

Similar Datasets

Unknown Enzymatic depilation of animal hide: identification of elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a depilating protease.
| S-EPMC3037957 | biostudies-literature
Unknown Analysis of the Pseudomonas aeruginosa elastase (lasB) regulatory region.
| S-EPMC177776 | biostudies-other
Unknown The Pseudomonas aeruginosa protease LasB directly activates IL-1β.
| S-EPMC7511813 | biostudies-literature
Unknown Inhibitors of the Elastase LasB for the Treatment of <i>Pseudomonas aeruginosa</i> Lung Infections.
| S-EPMC10755728 | biostudies-literature
Unknown The Structures and Binding Modes of Small-Molecule Inhibitors of <i>Pseudomonas aeruginosa</i> Elastase LasB.
| S-EPMC9404851 | biostudies-literature
Unknown Design of a gold nanoprobe for the detection of <i>Pseudomonas aeruginosa</i> elastase gene (lasB).
| S-EPMC9051652 | biostudies-literature
Unknown Higher levels of Pseudomonas aeruginosa LasB elastase expression are associated with early-stage infection in cystic fibrosis patients.
| S-EPMC10468528 | biostudies-literature
Unknown Chemical Optimization of Selective <i>Pseudomonas aeruginosa</i> LasB Elastase Inhibitors and Their Impact on LasB-Mediated Activation of IL-1β in Cellular and Animal Infection Models.
| S-EPMC9926489 | biostudies-literature
Unknown Molecular Analysis of the Contribution of Alkaline Protease A and Elastase B to the Virulence of <i>Pseudomonas aeruginosa</i> Bloodstream Infections.
| S-EPMC8823171 | biostudies-literature
Unknown VE-cadherin cleavage by LasB protease from Pseudomonas aeruginosa facilitates type III secretion system toxicity in endothelial cells.
| S-EPMC3953407 | biostudies-literature