Unknown

Dataset Information

0

A structurally unrelated mimic of a Pseudomonas aeruginosa acyl-homoserine lactone quorum-sensing signal.


ABSTRACT: The pathogenic bacterium Pseudomonas aeruginosa uses acyl-homoserine lactone quorum-sensing signals to coordinate the expression of a battery of virulence genes in a cascade of regulatory events. The quorum-sensing signal that triggers the cascade is N-3-oxo-dodecanoyl homoserine lactone (3OC12-HSL), which interacts with two signal receptor-transcription factors, LasR and QscR. This signal is base labile, and it is degraded by mammalian PON lactonases. We have identified a structurally unrelated triphenyl mimic of 3OC12-HSL that is base-insensitive and PON-resistant. The triphenyl mimic seems to interact specifically with LasR but not with QscR. In silico analysis suggests that the mimic fits into the 3OC12-HSL-binding site of LasR and makes key contacts with LasR. The triphenyl mimic is an excellent scaffold for developing quorum-sensing inhibitors, and its stability and potency make it ideal for biotechnology uses such as heterologous gene expression.

SUBMITTER: Muh U 

PROVIDER: S-EPMC1636559 | biostudies-literature | 2006 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

A structurally unrelated mimic of a Pseudomonas aeruginosa acyl-homoserine lactone quorum-sensing signal.

Müh Ute U   Hare Brian J BJ   Duerkop Breck A BA   Schuster Martin M   Hanzelka Brian L BL   Heim Roger R   Olson Eric R ER   Greenberg E Peter EP  

Proceedings of the National Academy of Sciences of the United States of America 20061030 45


The pathogenic bacterium Pseudomonas aeruginosa uses acyl-homoserine lactone quorum-sensing signals to coordinate the expression of a battery of virulence genes in a cascade of regulatory events. The quorum-sensing signal that triggers the cascade is N-3-oxo-dodecanoyl homoserine lactone (3OC12-HSL), which interacts with two signal receptor-transcription factors, LasR and QscR. This signal is base labile, and it is degraded by mammalian PON lactonases. We have identified a structurally unrelated  ...[more]

Similar Datasets

| S-EPMC6948153 | biostudies-literature
| S-EPMC3019841 | biostudies-literature
| S-EPMC7157775 | biostudies-literature
| S-EPMC3379639 | biostudies-literature
| S-EPMC3907830 | biostudies-other
| S-EPMC2546487 | biostudies-literature
| S-EPMC94816 | biostudies-literature
| S-EPMC4169570 | biostudies-literature
| S-EPMC4244979 | biostudies-literature
| S-EPMC1418629 | biostudies-literature