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  • Quorum sensing-dependent regulation and blockade of exoprotease production in Aeromonas hydrophila.

Quorum sensing-dependent regulation and blockade of exoprotease production in Aeromonas hydrophila.

Infection and immunity (1999-09-25)
S Swift, M J Lynch, L Fish, D F Kirke, J M Tomás, G S Stewart, P Williams
ABSTRACT

In Aeromonas hydrophila, the ahyI gene encodes a protein responsible for the synthesis of the quorum sensing signal N-butanoyl-L-homoserine lactone (C4-HSL). Inactivation of the ahyI gene on the A. hydrophila chromosome abolishes C4-HSL production. The exoprotease activity of A. hydrophila consists of both serine protease and metalloprotease activities; in the ahyI-negative strain, both are substantially reduced but can be restored by the addition of exogenous C4-HSL. In contrast, mutation of the LuxR homolog AhyR results in the loss of both exoprotease activities, which cannot be restored by exogenous C4-HSL. Furthermore, a substantial reduction in the production of exoprotease by the ahyI+ parent strain is obtained by the addition of N-acylhomoserine lactone analogs that have acyl side chains of 10, 12, or 14 carbons. The inclusion of N-(3-oxododecanoyl)-L-homoserine lactone or N-(3-oxotetradecanoyl)-L-homoserine lactone at 10 microM in overnight cultures of A. hydrophila abolishes exoprotease production in azocasein assays and reduces the activity of all the exoprotease species seen in zymograms.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
N-Octanoyl-DL-homoserine lactone, ≥97.0% (HPLC)
Sigma-Aldrich
N-Tetradecanoyl-DL-homoserine lactone, ≥97.0% (HPLC)
Sigma-Aldrich
N-(3-Oxodecanoyl)-L-homoserine lactone
Sigma-Aldrich
N-(3-Oxotetradecanoyl)-L-homoserine lactone
Sigma-Aldrich
N-Dodecanoyl-DL-homoserine lactone, ≥97.0% (HPLC)
Sigma-Aldrich
N-Heptanoyl-DL-homoserine lactone, ≥97.0% (HPLC)
Sigma-Aldrich
N-(3-Oxododecanoyl)-L-homoserine lactone, quorum sensing signaling molecule
Sigma-Aldrich
N-Decanoyl-DL-homoserine lactone, ≥97.0% (HPLC)