keratitis/protease

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Pseudomonas aeruginosa MucD protease mediates keratitis by inhibiting neutrophil recruitment and promoting bacterial survival.

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OBJECTIVE Pseudomonas aeruginosa is a leading pathogen of blinding keratitis worldwide. In this study, the role of the serine protease in the pathogenesis of P. aeruginosa keratitis in the mouse cornea was investigated by comparing the parent and rescue strains. METHODS Cornea of C57BL/6 mice were

Purification and characterization of a 33 kDa serine protease from Acanthamoeba lugdunensis KA/E2 isolated from a Korean keratitis patient.

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In order to evaluate the possible roles of secretory proteases in the pathogenesis of amoebic keratitis, we purified and characterized a serine protease secreted by Acanthamoeba lugdunensis KA/E2, isolated from a Korean keratitis patient. The ammonium sulfate-precipitated culture supernatant of the

The serratial 56K protease as a major pathogenic factor in serratial keratitis. Clinical and experimental study.

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A possible cause and the difference in clinical severity of serratial keratitis were investigated. Two strains of Serratia marcescens were isolated: one from a patient with severe liquefactive keratitis, who had diabetes mellitus, and one from a patient with mild superficial keratitis, but who had

Pseudomonas keratitis. The role of an uncharacterized exoprotein, protease IV, in corneal virulence.

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OBJECTIVE The role of exoproteins in the pathogenesis of Pseudomonas aeruginosa keratitis was investigated in three animal models by assessing the relationship between corneal virulence and the activities of exotoxin A, elastase, alkaline protease, and an uncharacterized protease, protease

Relationship between proteases and descemetocele formation in experimental Pseudomonas keratitis.

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Proteases are involved in the pathogenesis of Pseudomonas aeruginosa infections of the cornea. Although there are many potential roles for these enzymes, involvement in corneal stroma destruction with subsequent descemetocele formation and/or corneal perforation is an important example. This study

Immunization against experimental Pseudomonas aeruginosa and Serratia marcescens keratitis. Vaccination with lipopolysaccharide endotoxins and proteases.

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Rabbits vaccinated with lipopolysaccharide endotoxins or with purified protease preparations from Pseudomonas aeruginosa and Serratia marcescens before corneal challenge with the viable bacteria exhibited significantly less corneal damage than rabbits not vaccinated with the bacterial products.

Extracellular proteases of Aspergillus flavus. Fungal keratitis, proteases, and pathogenesis.

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To get a better understanding of the possible role of proteases in the pathogenesis of fungal keratitis, the extracellular proteases of a clinical isolate of Aspergillus flavus, from a severe case of keratitis, were identified and partially characterized. This strain, designated CU226/88, was grown

Role of contact lens wear, bacterial flora, and mannose-induced pathogenic protease in the pathogenesis of amoebic keratitis.

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The ocular surface is continuously exposed to potential pathogens, including free-living amoebae. Acanthamoeba species are among the most ubiquitous amoebae, yet Acanthamoeba keratitis is remarkably rare. The pathogenesis of Acanthamoeba keratitis is a complex, sequential process. Here we show that

Pseudomonas aeruginosa small protease (PASP), a keratitis virulence factor.

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OBJECTIVE The virulence contribution of Pseudomonas aeruginosa small protease (PASP) during experimental keratitis was studied by comparing a PASP-deficient mutant with its parent and rescue strains. METHODS The pasP gene of P. aeruginosa was replaced with the tetracycline resistance gene via

Type III secretion system-associated toxins, proteases, serotypes, and antibiotic resistance of Pseudomonas aeruginosa isolates associated with keratitis.

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The association between possession of toxin gene-related type III secretory system, protease profiles, O serotypes, and antibiotic resistance patterns was characterized genetically and phenotypically in 46 keratitis isolates of Pseudomonas aeruginosa. There was no significant difference in exoU or

Characterization of rabbit corneal damage produced by Serratia keratitis and by a serratia protease.

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The structural alterations elicited in the rabbit corneal stroma by experimental Serratia marcescens keratitis and by a highly purified serratia protease preparation were compared by gross observation, biochemical analyses, and electron microscopic examination of the affected tissue. Acute

Pseudomonas aeruginosa Keratitis: Protease IV and PASP as Corneal Virulence Mediators.

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Pseudomonas aeruginosa is a leading cause of bacterial keratitis, especially in users of contact lenses. These infections are characterized by extensive degradation of the corneal tissue mediated by Pseudomonas protease activities, including both Pseudomonas protease IV (PIV)

Pseudomonas aeruginosa LasA protease in treatment of experimental staphylococcal keratitis.

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LasA protease is a staphylolytic endopeptidase secreted by Pseudomonas aeruginosa. We have examined the effectiveness of LasA protease in the treatment of staphylococcal keratitis caused by methicillin-sensitive Staphylococcus aureus (MSSA) and methicillin-resistant S. aureus (MRSA) isolates in a

Role of bacterial proteases in pseudomonal and serratial keratitis.

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Pseudomonas aeruginosa and Serratia marcescens can cause refractory keratitis resulting in corneal perforation and blindness. These bacteria produce various kinds of proteases. In addition to pseudomonal elastase (LasB) and alkaline protease, LasA protease and protease IV have recently been found to

Pseudomonas keratitis: protease IV gene conservation, distribution, and production relative to virulence and other Pseudomonas proteases.

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OBJECTIVE To determine the distribution of the protease IV gene, the production of this and other proteases by multiple strains of Pseudomonas, and the virulence of a mutant specifically deficient in protease IV. METHODS The protease IV gene was cloned, its sequence analyzed, and its chromosomal

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