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Functional Genetic Analysis Reveals a 2-Alkyl-4-Quinolone Signaling System in the Human Pathogen Burkholderia pseudomallei and Related Bacteria.

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Functional Genetic Analysis Reveals a 2-Alkyl-4-Quinolone Signaling System in the Human Pathogen Burkholderia pseudomallei and Related Bacteria. / Diggle, Stephen P.; Lumjiaktase, Putthapoom; Dipilato, Francesca et al.
In: Chemistry and Biology, Vol. 13, No. 7, 07.2006, p. 701-710.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Diggle, SP, Lumjiaktase, P, Dipilato, F, Winzer, K, Kunakorn, M, Barrett, DA, Ram Chhabra, S, Cámara, M & Williams, P 2006, 'Functional Genetic Analysis Reveals a 2-Alkyl-4-Quinolone Signaling System in the Human Pathogen Burkholderia pseudomallei and Related Bacteria.', Chemistry and Biology, vol. 13, no. 7, pp. 701-710. https://doi.org/10.1016/j.chembiol.2006.05.006

APA

Diggle, S. P., Lumjiaktase, P., Dipilato, F., Winzer, K., Kunakorn, M., Barrett, D. A., Ram Chhabra, S., Cámara, M., & Williams, P. (2006). Functional Genetic Analysis Reveals a 2-Alkyl-4-Quinolone Signaling System in the Human Pathogen Burkholderia pseudomallei and Related Bacteria. Chemistry and Biology, 13(7), 701-710. https://doi.org/10.1016/j.chembiol.2006.05.006

Vancouver

Diggle SP, Lumjiaktase P, Dipilato F, Winzer K, Kunakorn M, Barrett DA et al. Functional Genetic Analysis Reveals a 2-Alkyl-4-Quinolone Signaling System in the Human Pathogen Burkholderia pseudomallei and Related Bacteria. Chemistry and Biology. 2006 Jul;13(7):701-710. doi: 10.1016/j.chembiol.2006.05.006

Author

Diggle, Stephen P. ; Lumjiaktase, Putthapoom ; Dipilato, Francesca et al. / Functional Genetic Analysis Reveals a 2-Alkyl-4-Quinolone Signaling System in the Human Pathogen Burkholderia pseudomallei and Related Bacteria. In: Chemistry and Biology. 2006 ; Vol. 13, No. 7. pp. 701-710.

Bibtex

@article{2ab9e93d44414052bcbb953f6908d489,
title = "Functional Genetic Analysis Reveals a 2-Alkyl-4-Quinolone Signaling System in the Human Pathogen Burkholderia pseudomallei and Related Bacteria.",
abstract = "Pseudomonas aeruginosa synthesizes diverse 2-alkyl-4(1H)-quinolones (AHQs), including the signaling molecule 2-heptyl-3-hydroxy-4(1H)-quinolone (PQS), via the pqsABCDE locus. By examining the genome databases, homologs of the pqs genes were identified in other bacteria. However, apart from P. aeruginosa, only Burkholderia pseudomallei and B. thailandensis contained a complete pqsA–E operon (termed hhqA–E). By introducing the B. pseudomallei hhqA and hhqE genes into P. aeruginosa pqsA and pqsE mutants, we show that they are functionally conserved and restore virulence factor and PQS production. B. pseudomallei, B. thailandensis, B. cenocepacia, and P. putida each produced 2-heptyl-4(1H)-quinolone (HHQ), but not PQS. Mutation of hhqA in B. pseudomallei resulted in the loss of AHQ production, altered colony morphology, and enhanced elastase production, which was reduced to parental levels by exogenous HHQ. These data reveal a role for AHQs in bacterial cell-to-cell communication beyond that seen in P. aeruginosa.",
keywords = "MICROBIO, SIGNALING, CHEMBIO",
author = "Diggle, {Stephen P.} and Putthapoom Lumjiaktase and Francesca Dipilato and Klaus Winzer and Mongkol Kunakorn and Barrett, {David A.} and {Ram Chhabra}, Siri and Miguel C{\'a}mara and Paul Williams",
year = "2006",
month = jul,
doi = "10.1016/j.chembiol.2006.05.006",
language = "English",
volume = "13",
pages = "701--710",
journal = "Chemistry and Biology",
issn = "1074-5521",
publisher = "Cell Press",
number = "7",

}

RIS

TY - JOUR

T1 - Functional Genetic Analysis Reveals a 2-Alkyl-4-Quinolone Signaling System in the Human Pathogen Burkholderia pseudomallei and Related Bacteria.

AU - Diggle, Stephen P.

AU - Lumjiaktase, Putthapoom

AU - Dipilato, Francesca

AU - Winzer, Klaus

AU - Kunakorn, Mongkol

AU - Barrett, David A.

AU - Ram Chhabra, Siri

AU - Cámara, Miguel

AU - Williams, Paul

PY - 2006/7

Y1 - 2006/7

N2 - Pseudomonas aeruginosa synthesizes diverse 2-alkyl-4(1H)-quinolones (AHQs), including the signaling molecule 2-heptyl-3-hydroxy-4(1H)-quinolone (PQS), via the pqsABCDE locus. By examining the genome databases, homologs of the pqs genes were identified in other bacteria. However, apart from P. aeruginosa, only Burkholderia pseudomallei and B. thailandensis contained a complete pqsA–E operon (termed hhqA–E). By introducing the B. pseudomallei hhqA and hhqE genes into P. aeruginosa pqsA and pqsE mutants, we show that they are functionally conserved and restore virulence factor and PQS production. B. pseudomallei, B. thailandensis, B. cenocepacia, and P. putida each produced 2-heptyl-4(1H)-quinolone (HHQ), but not PQS. Mutation of hhqA in B. pseudomallei resulted in the loss of AHQ production, altered colony morphology, and enhanced elastase production, which was reduced to parental levels by exogenous HHQ. These data reveal a role for AHQs in bacterial cell-to-cell communication beyond that seen in P. aeruginosa.

AB - Pseudomonas aeruginosa synthesizes diverse 2-alkyl-4(1H)-quinolones (AHQs), including the signaling molecule 2-heptyl-3-hydroxy-4(1H)-quinolone (PQS), via the pqsABCDE locus. By examining the genome databases, homologs of the pqs genes were identified in other bacteria. However, apart from P. aeruginosa, only Burkholderia pseudomallei and B. thailandensis contained a complete pqsA–E operon (termed hhqA–E). By introducing the B. pseudomallei hhqA and hhqE genes into P. aeruginosa pqsA and pqsE mutants, we show that they are functionally conserved and restore virulence factor and PQS production. B. pseudomallei, B. thailandensis, B. cenocepacia, and P. putida each produced 2-heptyl-4(1H)-quinolone (HHQ), but not PQS. Mutation of hhqA in B. pseudomallei resulted in the loss of AHQ production, altered colony morphology, and enhanced elastase production, which was reduced to parental levels by exogenous HHQ. These data reveal a role for AHQs in bacterial cell-to-cell communication beyond that seen in P. aeruginosa.

KW - MICROBIO

KW - SIGNALING

KW - CHEMBIO

U2 - 10.1016/j.chembiol.2006.05.006

DO - 10.1016/j.chembiol.2006.05.006

M3 - Journal article

VL - 13

SP - 701

EP - 710

JO - Chemistry and Biology

JF - Chemistry and Biology

SN - 1074-5521

IS - 7

ER -