N-acyl homoserine lactones are degraded via an amidolytic activity in Comamonas sp. strain D1.
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.
Uroz
Stéphane
S
CNRS, ISV, Bâtiment 23, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
Oger
Phil
P
Chhabra
Siri Ram
SR
Cámara
Miguel
M
Williams
Paul
P
Dessaux
Yves
Y
D015107:4-Butyrolactone / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D020585:Comamonas / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D010088:Oxidoreductases / Q000378:metabolism*; D053038:Quorum Sensing
C088386:homoserine lactone; D010088:Oxidoreductases; D015107:4-Butyrolactone