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Infection and Immunity, October 1999, p. 5192-5199, Vol. 67, No. 10
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Quorum Sensing-Dependent Regulation and Blockade of Exoprotease Production in Aeromonas hydrophila

Simon Swift,1,2,* Martin J. Lynch,1,2 Leigh Fish,2,dagger David F. Kirke,1,2 Juan M. Tomás,3 Gordon S. A. B. Stewart,2 and Paul Williams1,2,4

Institute of Infections and Immunity1 and School of Clinical Laboratory Sciences,4 Queen's Medical Centre, University of Nottingham, Nottingham, NG7 2UH, and School of Pharmaceutical Sciences, University Park, University of Nottingham, Nottingham, NG7 2RD,2 United Kingdom, and Departmento de Microbiología, Facultad de Biología, Universidad de Barcelona, 08071 Barcelona, Spain3

Received 22 March 1999/Returned for modification 14 May 1999/Accepted 27 July 1999

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 µM in overnight cultures of A. hydrophila abolishes exoprotease production in azocasein assays and reduces the activity of all the exoprotease species seen in zymograms.

* Corresponding author. Mailing address: Institute of Infections and Immunity, C-Floor, West Block, Queen's Medical Centre, University of Nottingham, Nottingham, NG7 2UH, United Kingdom. Phone: 44 (115) 9249924, ext. 42454. Fax: 44 (115) 9709923. E-mail: simon.swift{at}nottingham.ac.uk.

dagger Present address: Explore@Bristol, Harbourside, Bristol BS1 5DB, United Kingdom.

Infection and Immunity, October 1999, p. 5192-5199, Vol. 67, No. 10
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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