Title:

Enzymatic degradation of acyl-homoserine lactones and its possible use in biocontrol and suppression of infection development

Subtitle:

Enzymatic degradation of acyl-homoserine lactones and its possible use in biocontrol and suppression of infection development

Creator:

Czajkowski, Robert ; Jafra, Sylwia

Publisher:

Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS

Date issued/created:

2006

Subject and Keywords:

biotechnology

Abstract:

A large number of different bacteria populations control diverse metabolic processes through production and distribution of specific signal molecules, which concentration in the environment depends on bacteria cell density and rise when bacteria population expands. This strategy is known as quorum sensing (QS), and was first described in Gram-negative, marine bacterium Vibrio fischeh. QS, a mechanism of gene expression regulation dependent on bacteria cell density, is widely distributed in Gram-negative bacteria; and controls different physiological processes such as production of virulence factors, conjugal plasmid transfer, antibiotic production, replication, swarming or luminescence. QS functions via signal molecules: in Gram-negative bacteria, the signal molecules belong to the acyl-homoserine lactones (AHLs). It was found that many bacteria possess the ability to interfere in QS (strategy known as quorum quenching- QQ) by enzymatic degradation of AHLs. Till now, two classes of enzymes able to degrade AHLs have been described: AHL-lactonases and AHL-acylases. AHL-lactonases hydrolyze the ester bond in the lactone ring of AHLs. AHL- -acylases hydrolyze the amide bond between the acyl side chain and the lactone ring in AHLs. Both reactions lead to the inhibition of signal transfer in QS as degradation products cannot act as signal molecules. QS plays a major role in pathogenesis and as such is deeply studied as a useful target for modern, antimicrobial therapy in human medicine and veterinary, as well as in biocontrol of plant diseases.

Relation:

Biotechnologia, vol.73, 2 (2006)-.

Volume:

73

Issue:

2

Start page:

49

End page:

64

Resource type:

Text

Detailed Resource Type:

Article

Format:

application/pdf

Resource Identifier:

0860-7796 ; IChB B-69

Source:

Library of Institute of Bioorganic Chemistry PAS

Language:

pol

Language of abstract:

eng

Temporal coverage:

1988-2010

Rights:

Creative Commons Attribution BY-SA 4.0 license

Terms of use:

Copyright-protected material. [CC BY-SA 4.0] May be used within the scope specified in Creative Commons Attribution BY-SA 4.0 license, full text available at:

Digitizing institution:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Original in:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Projects co-financed by:

Operational Program Digital Poland, 2014-2020, Measure 2.3: Digital accessibility and usefulness of public sector information; funds from the European Regional Development Fund and national co-financing from the state budget.

Access:

Open