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• W2075344546 startingPage "695" @default.
• W2075344546 abstract "Aims: To identify enzymes associated with bacteriophages infecting cystic fibrosis (CF) strains of Pseudomonas aeruginosa that are able to degrade extracellular alginic acids elaborated by the host bacterium. Methods and Results: Plaques produced by 21 Ps. aeruginosa-specific phages were screened for the presence of haloes, an indicator of capsule hydrolytic activity. Four phages produced haloed plaques, and one (PT-6) was investigated further. PT-6 was shown by electron microscopy to belong to Podoviridae family C1, to reduce the viscosity of four alginate preparations using a rolling ball viscometer and to release uronic acid-containing fragments from the polymers, as judged by spectrophotometry and thin layer chromatography. The alginase was partially purified by gel filtration chromatography and shown to be a 37 kDa polypeptide. Conclusions: Infection of CF strains of Ps. aeruginosa by phage PT-6 involves hydrolysis of the exopolysaccharide secreted by the host. Significance and Impact of the Study: The alginase produced by PT-6 has the potential to increase the well-being of CF suffers by improving the surface properties of sputum, accelerating phagocytic uptake of bacteria and perturbing bacterial growth in biofilms." @default.
• W2075344546 created "2016-06-24" @default.
• W2075344546 creator A5015518286 @default.
• W2075344546 creator A5072319145 @default.
• W2075344546 creator A5091567583 @default.
• W2075344546 date "2010-02-01" @default.
• W2075344546 modified "2023-09-26" @default.
• W2075344546 title "Bacteriophage-derived enzyme that depolymerizes the alginic acid capsule associated with cystic fibrosis isolates of<i>Pseudomonas aeruginosa</i>" @default.
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• W2075344546 doi "https://doi.org/10.1111/j.1365-2672.2009.04469.x" @default.
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