N-acyl homoserine lactones are degraded via an amidolytic activity in Comamonas sp. strain D1. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Archives of Microbiology Année : 2006

N-acyl homoserine lactones are degraded via an amidolytic activity in Comamonas sp. strain D1.

Résumé

ABTSRACT: Comamonas strain D1 enzymatically inactivates quorum-sensing (QS) signal molecules of the N-acyl homoserine lactone (N-AHSL) family, and exhibits the broadest inactivation range of known bacteria. It degrades N-AHSL with acyl-side chains ranging from 4 to 16 carbons, with or without 3-oxo or 3-hydroxy substitutions. N-AHSL degradation yields HSL but not N-acyl homoserine: strain D1 therefore harbors an amidohydrolase activity. Strain D1 is the fifth bacterium species in which an N-AHSL amidohydrolase is described. Consistent with its N-AHSL degradation ability, strain D1 efficiently quenches various QS-dependent functions in other bacteria, such as violacein production by Chromobacterium violaceum and pathogenicity and antibiotic production in Pectobacterium.

Dates et versions

hal-00119105 , version 1 (07-12-2006)

Identifiants

Citer

Stéphane Uroz, Yves Dessaux, Philippe M. Oger, Siri Ram Chhabra, Miguel Cámara, et al.. N-acyl homoserine lactones are degraded via an amidolytic activity in Comamonas sp. strain D1.. Archives of Microbiology, 2006, 187 (3), pp.249-256. ⟨10.1007/s00203-006-0186-5⟩. ⟨hal-00119105⟩
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