Orally Administered ThermostableN-Acyl Homoserine Lactonase from Bacillus sp. Strain AI96 Attenuates Aeromonas hydrophila Infection in Zebrafish
ABSTRACTN-Acylated homoserine lactone (AHL) lactonases are capable of degrading signal molecules involved in bacterial quorum sensing and therefore represent a new approach to control bacterial infection. Here a gene responsible for the AHL lactonase activity ofBacillussp. strain AI96, 753 bp in length, was cloned and then expressed inEscherichia coli. The deduced amino acid sequence ofBacillussp. AI96 AiiA (AiiAAI96) is most similar to those of otherBacillussp. AHL lactonases (∼80% sequence identity) and was consequently categorized as a member of the metallo-β-lactamase superfamily. AiiAAI96maintains ∼100% of its activity at 10°C to 40°C at pH 8.0, and it is very stable at 70°C at pH 8.0 for at least 1 h; no otherBacillusAHL lactonase has been found to be stable under these conditions. AiiAAI96resists digestion by proteases and carp intestinal juice, and it has broad-spectrum substrate specificity. The supplementation of AiiAAI96into fish feed by oral administration significantly attenuatedAeromonas hydrophilainfection in zebrafish. This is the first report of the oral administration of an AHL lactonase for the efficient control ofA. hydrophila.