Document Type

Article

Publication Date

1-2013

Publication Title

Antimicrobial Agents and Chemotherapy

Department

Thayer School of Engineering

Abstract

More than 2 decades of study support the hypothesis that alginate lyases are promising therapeutic candidates for treating mucoid Pseudomonas aeruginosa infections. In particular, the enzymes' ability to degrade alginate, a key component of mucoid biofilm matrix, has been the presumed mechanism by which they disrupt biofilms and enhance antibiotic efficacy. The systematic studies reported here show that, in an in vitro model, alginate lyase dispersion of P. aeruginosa biofilms and enzyme synergy

DOI

10.1128/AAC.01789-12

Comments

More than 2 decades of study support the hypothesis that alginate lyases are promising therapeutic candidates for treating mu- coid Pseudomonas aeruginosa infections. In particular, the enzymes’ ability to degrade alginate, a key component of mucoid bio- film matrix, has been the presumed mechanism by which they disrupt biofilms and enhance antibiotic efficacy. The systematic studies reported here show that, in an in vitro model, alginate lyase dispersion of P. aeruginosa biofilms and enzyme synergy with tobramycin are completely decoupled from catalytic activity. In fact, equivalent antibiofilm effects can be achieved with bovine serum albumin or simple amino acids. These results provide new insights into potential mechanisms of alginate lyase therapeutic activity, and they should motivate a careful reexamination of the fundamental assumptions underlying interest in enzymatic biofilm dispersion.

Original Citation

Lamppa JW, Griswold KE. Alginate lyase exhibits catalysis-independent biofilm dispersion and antibiotic synergy. Antimicrob Agents Chemother. 2013 Jan;57(1):137-45. doi: 10.1128/AAC.01789-12. Epub 2012 Oct 15. PMID: 23070175; PMCID: PMC3535929.

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