Structure-function analysis of the C-3 position in analogues of microbial behavioural modulators HHQ and PQS

2-Heptyl-3-hydroxy-4-quinolone (PQS) and its precursor 2-heptyl-4-quinolone (HHQ) are key signalling molecules of the important nosocomial pathogen Pseudomonas aeruginosa. We have recently reported an interkingdom dimension to these molecules, influencing key virulence traits in a broad spectrum of...

Full description

Bibliographic Details
Main Authors: Reen, F., Clarke, S., Legendre, C., McSweeney, C., Eccles, K., Lawrence, S., O'Gara, Fergal, McGlacken, G.
Format: Journal Article
Published: Royal Society of Chemistry 2012
Online Access:http://hdl.handle.net/20.500.11937/19919
_version_ 1848750165525004288
author Reen, F.
Clarke, S.
Legendre, C.
McSweeney, C.
Eccles, K.
Lawrence, S.
O'Gara, Fergal
McGlacken, G.
author_facet Reen, F.
Clarke, S.
Legendre, C.
McSweeney, C.
Eccles, K.
Lawrence, S.
O'Gara, Fergal
McGlacken, G.
author_sort Reen, F.
building Curtin Institutional Repository
collection Online Access
description 2-Heptyl-3-hydroxy-4-quinolone (PQS) and its precursor 2-heptyl-4-quinolone (HHQ) are key signalling molecules of the important nosocomial pathogen Pseudomonas aeruginosa. We have recently reported an interkingdom dimension to these molecules, influencing key virulence traits in a broad spectrum of microbial species and in the human pathogenic yeast Candida albicans. For the first time, targeted chemical derivatisation of the C-3 position was undertaken to investigate the structural and molecular properties underpinning the biological activity of these compounds in P. aeruginosa, and using Bacillus subtilis as a suitable model system for investigating modulation of interspecies behaviour.
first_indexed 2025-11-14T07:32:30Z
format Journal Article
id curtin-20.500.11937-19919
institution Curtin University Malaysia
institution_category Local University
last_indexed 2025-11-14T07:32:30Z
publishDate 2012
publisher Royal Society of Chemistry
recordtype eprints
repository_type Digital Repository
spelling curtin-20.500.11937-199192017-09-13T13:51:03Z Structure-function analysis of the C-3 position in analogues of microbial behavioural modulators HHQ and PQS Reen, F. Clarke, S. Legendre, C. McSweeney, C. Eccles, K. Lawrence, S. O'Gara, Fergal McGlacken, G. 2-Heptyl-3-hydroxy-4-quinolone (PQS) and its precursor 2-heptyl-4-quinolone (HHQ) are key signalling molecules of the important nosocomial pathogen Pseudomonas aeruginosa. We have recently reported an interkingdom dimension to these molecules, influencing key virulence traits in a broad spectrum of microbial species and in the human pathogenic yeast Candida albicans. For the first time, targeted chemical derivatisation of the C-3 position was undertaken to investigate the structural and molecular properties underpinning the biological activity of these compounds in P. aeruginosa, and using Bacillus subtilis as a suitable model system for investigating modulation of interspecies behaviour. 2012 Journal Article http://hdl.handle.net/20.500.11937/19919 10.1039/c2ob26823j Royal Society of Chemistry restricted
spellingShingle Reen, F.
Clarke, S.
Legendre, C.
McSweeney, C.
Eccles, K.
Lawrence, S.
O'Gara, Fergal
McGlacken, G.
Structure-function analysis of the C-3 position in analogues of microbial behavioural modulators HHQ and PQS
title Structure-function analysis of the C-3 position in analogues of microbial behavioural modulators HHQ and PQS
title_full Structure-function analysis of the C-3 position in analogues of microbial behavioural modulators HHQ and PQS
title_fullStr Structure-function analysis of the C-3 position in analogues of microbial behavioural modulators HHQ and PQS
title_full_unstemmed Structure-function analysis of the C-3 position in analogues of microbial behavioural modulators HHQ and PQS
title_short Structure-function analysis of the C-3 position in analogues of microbial behavioural modulators HHQ and PQS
title_sort structure-function analysis of the c-3 position in analogues of microbial behavioural modulators hhq and pqs
url http://hdl.handle.net/20.500.11937/19919