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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.

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