Glonti, T., Chanishvili, N. and Taylor, P.W. (2010) Bacteriophage-derived enzyme that depolymerizes the alginic acid capsule associated with cystic fibrosis isolates ofPseudomonas aeruginosa. Journal of Applied Microbiology, 108 (2). pp. 695-702. 10.1111/j.1365-2672.2009.04469.x.
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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.
|Uncontrolled Keywords:||alginate lyase;alginic acid;bacteriophage;exopolysaccharide depolymerase;Pseudomonas aeruginosa|
|Departments, units and centres:||Department of Pharmaceutics > Department of Pharmaceutics|
|Journal or Publication Title:||Journal of Applied Microbiology|
|Deposited By:||Library Staff|
|Deposited On:||12 Jan 2012 13:59|
|Last Modified:||12 Jan 2012 13:59|
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