A @entity796 isolated from a contact lens-induced acute red eye ( XXXX ) is protease-deficient.

@entity2194 @entity796 @entity1036 @entity19 @entity1066 @entity281 @entity2687 @entity325
PURPOSE: @entity796 proteases are thought to be important virulence factors in the pathogenesis of @entity2687 . This study examined protease production from two strains of @entity796 responsible for two very distinct clinical diseases: strain Paer1, isolated from a @entity2194 ( @entity2194 ), and strain KEI 1025, isolated from a corneal @entity1066 . Strains were compared to a laboratory strain (ATCC 19660) known to produce severe @entity1036 in experimentally infected @entity19 for protease production and for ocular virulence. METHODS: Protease production was examined with colorimetric assays, gelatin zymography and western blots. Elastase A activity was quantitated with a staphylolytic assay. Ocular virulence was examined using a @entity19 scratch model of @entity1036 . RESULTS: In contrast to strains KEI 1025 or ATCC 19660, Paer1 was unable to produce enzymatically active elastase A, elastase, and protease IV. All three strains produced active alkaline protease. Strains KEI 1025 and ATCC 19660 produced a fulminant @entity1036 in @entity19 whereas Paer1 produced a mild transient @entity281 . Restoration of elastase activity in Paer1 via genetic complementation did not result in a virulent phenotype. @entity325 of @entity19 eyes with strains Paer1 and ATCC 19660 resulted in the eventual loss of Paer1 from corneal tissue. CONCLUSIONS: These studies suggest that @entity796 elastase A and/or protease IV, but not alkaline protease or elastase, contribute to the ocular virulence of this organism.
