Biotic inactivation of the Pseudomonas aeruginosa quinolone signal molecule
In Pseudomonas aeruginosa, quorum sensing (QS) regulates the production of secondary metabolites, many of which are antimicrobials that impact on polymicrobial community composition. Consequently, quenching QS modulates the environmental impact of P. aeruginosa. To identify bacteria capable of inact...
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| Format: | Article |
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Wiley
2015
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| Online Access: | https://eprints.nottingham.ac.uk/34902/ |
| _version_ | 1848794958552629248 |
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| author | Soh, Eliza Ye-Chen Chhabra, Siri Ram Halliday, Nigel Heeb, Stephan Müller, Christine Birmes, Franziska S. Fetzner, Susanne Cámara, Miguel Chan, Kok Gan Williams, Paul |
| author_facet | Soh, Eliza Ye-Chen Chhabra, Siri Ram Halliday, Nigel Heeb, Stephan Müller, Christine Birmes, Franziska S. Fetzner, Susanne Cámara, Miguel Chan, Kok Gan Williams, Paul |
| author_sort | Soh, Eliza Ye-Chen |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | In Pseudomonas aeruginosa, quorum sensing (QS) regulates the production of secondary metabolites, many of which are antimicrobials that impact on polymicrobial community composition. Consequently, quenching QS modulates the environmental impact of P. aeruginosa. To identify bacteria capable of inactivating the QS signal molecule 2-heptyl-3- hydroxy-4(1H)-quinolone (PQS), a minimal medium containing PQS as the sole carbon source was used to enrich a Malaysian rainforest soil sample. This yielded an Achromobacter xylosoxidans strain (Q19) that inactivated PQS, yielding a new fluorescent compound (I-PQS) confirmed as PQS-derived using deuterated PQS. The I-PQS structure was elucidated using mass spectrometry and nuclear magnetic resonance spectroscopy as 2-heptyl-2-hydroxy-1,2-dihydroquinoline- 3,4-dione (HHQD). Achromobacter xylosoxidans Q19 oxidized PQS congeners with alkyl chains ranging from C1 to C5 and also N-methyl PQS, yielding the corresponding 2-hydroxy-1,2-dihydroquinoline-3,4- diones, but was unable to inactivate thePQSprecursor HHQ. This indicates that the hydroxyl group at position 3 in PQS is essential and that A. xylosoxidans inactivates PQS via a pathway involving the incorporation of oxygen at C2 of the heterocyclic ring. The conversion of PQS to HHQD also occurred on incubation with 12/17 A. xylosoxidans strains recovered from cystic fibrosis patients, with P. aeruginosa and with Arthrobacter, suggesting that formation of hydroxylated PQS may be a common mechanism of inactivation. |
| first_indexed | 2025-11-14T19:24:28Z |
| format | Article |
| id | nottingham-34902 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T19:24:28Z |
| publishDate | 2015 |
| publisher | Wiley |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-349022020-05-04T20:06:41Z https://eprints.nottingham.ac.uk/34902/ Biotic inactivation of the Pseudomonas aeruginosa quinolone signal molecule Soh, Eliza Ye-Chen Chhabra, Siri Ram Halliday, Nigel Heeb, Stephan Müller, Christine Birmes, Franziska S. Fetzner, Susanne Cámara, Miguel Chan, Kok Gan Williams, Paul In Pseudomonas aeruginosa, quorum sensing (QS) regulates the production of secondary metabolites, many of which are antimicrobials that impact on polymicrobial community composition. Consequently, quenching QS modulates the environmental impact of P. aeruginosa. To identify bacteria capable of inactivating the QS signal molecule 2-heptyl-3- hydroxy-4(1H)-quinolone (PQS), a minimal medium containing PQS as the sole carbon source was used to enrich a Malaysian rainforest soil sample. This yielded an Achromobacter xylosoxidans strain (Q19) that inactivated PQS, yielding a new fluorescent compound (I-PQS) confirmed as PQS-derived using deuterated PQS. The I-PQS structure was elucidated using mass spectrometry and nuclear magnetic resonance spectroscopy as 2-heptyl-2-hydroxy-1,2-dihydroquinoline- 3,4-dione (HHQD). Achromobacter xylosoxidans Q19 oxidized PQS congeners with alkyl chains ranging from C1 to C5 and also N-methyl PQS, yielding the corresponding 2-hydroxy-1,2-dihydroquinoline-3,4- diones, but was unable to inactivate thePQSprecursor HHQ. This indicates that the hydroxyl group at position 3 in PQS is essential and that A. xylosoxidans inactivates PQS via a pathway involving the incorporation of oxygen at C2 of the heterocyclic ring. The conversion of PQS to HHQD also occurred on incubation with 12/17 A. xylosoxidans strains recovered from cystic fibrosis patients, with P. aeruginosa and with Arthrobacter, suggesting that formation of hydroxylated PQS may be a common mechanism of inactivation. Wiley 2015-11 Article PeerReviewed Soh, Eliza Ye-Chen, Chhabra, Siri Ram, Halliday, Nigel, Heeb, Stephan, Müller, Christine, Birmes, Franziska S., Fetzner, Susanne, Cámara, Miguel, Chan, Kok Gan and Williams, Paul (2015) Biotic inactivation of the Pseudomonas aeruginosa quinolone signal molecule. Environmental Microbiology, 17 (11). pp. 4352-4365. ISSN 1462-2920 http://onlinelibrary.wiley.com/doi/10.1111/1462-2920.12857/abstract;jsessionid=C08BE6169024674AD160797ED1F1F8F3.f03t02 doi:10.1111/1462-2920.12857 doi:10.1111/1462-2920.12857 |
| spellingShingle | Soh, Eliza Ye-Chen Chhabra, Siri Ram Halliday, Nigel Heeb, Stephan Müller, Christine Birmes, Franziska S. Fetzner, Susanne Cámara, Miguel Chan, Kok Gan Williams, Paul Biotic inactivation of the Pseudomonas aeruginosa quinolone signal molecule |
| title | Biotic inactivation of the Pseudomonas aeruginosa quinolone signal molecule |
| title_full | Biotic inactivation of the Pseudomonas aeruginosa quinolone signal molecule |
| title_fullStr | Biotic inactivation of the Pseudomonas aeruginosa quinolone signal molecule |
| title_full_unstemmed | Biotic inactivation of the Pseudomonas aeruginosa quinolone signal molecule |
| title_short | Biotic inactivation of the Pseudomonas aeruginosa quinolone signal molecule |
| title_sort | biotic inactivation of the pseudomonas aeruginosa quinolone signal molecule |
| url | https://eprints.nottingham.ac.uk/34902/ https://eprints.nottingham.ac.uk/34902/ https://eprints.nottingham.ac.uk/34902/ |