melioidosis/protease

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Deficiency of protease-activated receptor-1 limits bacterial dissemination during severe Gram-negative sepsis (melioidosis).

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Protease-activated receptor-1 (PAR-1) is a G-coupled transmembrane receptor expressed by multiple cell types present in the lungs that can be activated by various proteases generated during acute inflammation. In this study we aimed to investigate the role of PAR-1 during melioidosis, a common cause

Diabetes-independent increase of factor VII-activating protease activation in patients with Gram-negative sepsis (melioidosis).

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BACKGROUND The plasma protease factor VII-activating protease (FSAP) can release nucleosomes from late apoptotic cells. Nucleosomes are markers of cell death, and extracellular cell-free DNA has been suggested to play an important role in inflammation and has been demonstrated to correlate with

Endogenous protein C has a protective role during Gram-negative pneumosepsis (melioidosis).

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BACKGROUND Activated protein C (APC) exerts anticoagulant effects via inactivation of factors Va and VIIIa and cytoprotective effects via protease activated receptor (PAR)1. Inhibition of endogenous APC in endotoxemia and sepsis results in exacerbation of coagulation and inflammation, with

The serine protease inhibitor Ecotin is required for full virulence of Burkholderia pseudomallei.

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Burkholderia pseudomallei is a Gram negative soil saprophyte that causes the disease melioidosis where clinical symptoms can vary from localised infection to pneumonia and septic shock. Ecotin is a potent periplasmic serine protease inhibitor first identified in Escherichia coli. Ecotin, although

Purification and characterization of a protease from Pseudomonas pseudomallei.

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Pseudomonas pseudomallei is the causative agent of melioidosis, a glanders-like disease of humans and animals. The pathogenesis of melioidosis is not well understood, and the role of various extracellular enzymes produced by P. pseudomallei in the development of this disease is not known. The

Overexpression of the endothelial protein C receptor is detrimental during pneumonia-derived gram-negative sepsis (Melioidosis).

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BACKGROUND The endothelial protein C receptor (EPCR) enhances anticoagulation by accelerating activation of protein C to activated protein C (APC) and mediates anti-inflammatory effects by facilitating APC-mediated signaling via protease activated receptor-1. We studied the role of EPCR in the host

Immunogenic recombinant Burkholderia pseudomallei MprA serine protease elicits protective immunity in mice.

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Burkholderia pseudomallei is resistant to a diverse group of antimicrobials including third generation cephalosporins whilst quinolones and aminoglycosides have no reliable effect. As therapeutic options are limited, development of more effective forms of immunotherapy is vital to avoid a fatal

Innate immune responses of pulmonary epithelial cells to Burkholderia pseudomallei infection.

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BACKGROUND Burkholderia pseudomallei, a facultative intracellular pathogen, causes systemic infection in humans with high mortality especially when infection occurs through an infectious aerosol. Previous studies indicated that the epithelial cells in the lung are an active participant in host

Curcumin rescues Caenorhabditis elegans from a Burkholderia pseudomallei infection.

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The tropical pathogen Burkholderia pseudomallei requires long-term parenteral antimicrobial treatment to eradicate the pathogen from an infected patient. However, the development of antibiotic resistance is emerging as a threat to this form of treatment. To meet the need for alternative

The PmlI-PmlR quorum-sensing system in Burkholderia pseudomallei plays a key role in virulence and modulates production of the MprA protease.

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Burkholderia pseudomallei is the causative agent of melioidosis, an often fatal infection of humans and animals. The virulence of this pathogen is thought to depend on a number of secreted proteins, including the MprA metalloprotease. We observed that MprA is produced upon entry into the stationary

[Pathogenicity of Burkholderia pseudomallei: extracellular and surface antigen functions].

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The data of literature and the results of investigations carried out by the authors on the analysis of B. pseudomallei pathogenicity factors. They include mucoid, endotoxin, lecithinase, proteases, hemolysins, etc. In addition to fimbriae and pili, the adhesive properties of B. pseudomallei are

Analysis of peptide mimotopes of Burkholderia pseudomallei exopolysaccharide.

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Previously two capsule-specific monoclonal antibodies (4VA5 and 3VIE5) were identified as protective against Burkholderia pseudomallei in passive transfer experiments. Panning these antibodies against evolutionary phage libraries identified reactive peptides capable of inhibiting its parent

Enzymatic and molecular characterisation of leucine aminopeptidase of Burkholderia pseudomallei.

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BACKGROUND Leucine aminopeptidase (LAP) has been known to be a housekeeping protease, DNA-binding protein and repressor or activator in the operon regulation of virulence-associated genes in several bacterial species. LAP activity was consistently detected in overnight cultures of Burkholderia

The Burkholderia pseudomallei oxyR gene: expression analysis and mutant characterization.

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Burkholderia pseudomallei (Bp) is the causative agent of the life-threatening melioidosis in humans. The global transcription factor oxyR gene was isolated and characterized. It is located between recG, encoding a putative DNA helicase, and katG, encoding a putative catalase-peroxidase. oxyR is

Enzymatic profiling of clinical and environmental isolates of Burkholderia pseudomallei.

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Melioidosis has been recognized as an important cause of sepsis in the tropics. The disease caused by an environmental saprophyte Burkholderia pseudomallei, affects mostly adults with underlying immunocompromised conditions. In this study, the enzymatic profiles of 91 clinical and 9 environmental

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