Journal article
Pyocyanin degradation by a tautomerizing demethylase inhibits Pseudomonas aeruginosa biofilms
- Abstract:
- The opportunistic pathogen Pseudomonas aeruginosa produces colorful redox-active metabolites called phenazines, which underpin biofilm development, virulence and clinical outcomes. Though phenazines exist in many forms, the best studied is pyocyanin. Here, we describe pyocyanin demethylase (PodA), a hitherto uncharacterized protein that oxidizes the pyocyanin methyl group to formaldehyde and reduces the pyrazine ring via an unusual tautomerizing demethylation reaction. Treatment with PodA disrupts P. aeruginosa biofilm formation similarly to DNase, suggesting interference with the pyocyanin-dependent release of extracellular DNA into the matrix. PodA-dependent pyocyanin demethylation also restricts established biofilm aggregate populations experiencing anoxic conditions. Together, these results show that modulating extracellular redox-active metabolites can influence the fitness of a biofilm-forming microorganism.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
-
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(Preview, Accepted manuscript, pdf, 20.0MB, Terms of use)
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- Publisher copy:
- 10.1126/science.aag3180
Authors
+ National Institutes of Health
More from this funder
- Funding agency for:
- Costa, K
- Grant:
- F32AI112248
- 5R01HL117328-03
- Publisher:
- American Association for the Advancement of Science
- Journal:
- Science More from this journal
- Volume:
- 355
- Issue:
- 6321
- Pages:
- 170-173
- Publication date:
- 2017-01-13
- Acceptance date:
- 2016-11-29
- DOI:
- EISSN:
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1095-9203
- ISSN:
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0036-8075
- Language:
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English
- Keywords:
- Pubs id:
-
pubs:666470
- UUID:
-
uuid:08ab931e-2dd1-4263-bb4b-1a8dfa5a8e71
- Local pid:
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pubs:666470
- Source identifiers:
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666470
- Deposit date:
-
2016-12-19
Terms of use
- Copyright holder:
- Copyright 2016 by the American Association for the Advancement of Science: all rights reserved
- Copyright date:
- 2017
- Notes:
-
This is
the author’s version of the work. It is posted here by permission of the AAAS for personal
use, not for redistribution. The definitive version was published in Science on
December 08, 2016 , DOI: 10.1126/science.aag3180
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