Orally Administered Thermostable N-Acyl Homoserine Lactonase from Bacillus sp Strain AI96 Attenuates Aeromonas hydrophila Infection in Zebrafish
文献类型: 外文期刊
第一作者: Cao, Yanan
作者: Cao, Yanan;He, Suxu;Zhou, Zhigang;Zhang, Meichao;Mao, Wei;Yao, Bin;Cao, Yanan;Zhang, Huitu
作者机构:
期刊名称:APPLIED AND ENVIRONMENTAL MICROBIOLOGY ( 影响因子:4.792; 五年影响因子:5.26 )
ISSN: 0099-2240
年卷期: 2012 年 78 卷 6 期
页码:
收录情况: SCI
摘要: N-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 of Bacillus sp. strain AI96, 753 bp in length, was cloned and then expressed in Escherichia coli. The deduced amino acid sequence of Bacillus sp. AI96 AiiA (AiiA(AI96)) is most similar to those of other Bacillus sp. AHL lactonases (similar to 80% sequence identity) and was consequently categorized as a member of the metallo-beta-lactamase superfamily. AiiA(AI96) maintains similar to 100% of its activity at 10 degrees C to 40 degrees C at pH 8.0, and it is very stable at 70 degrees C at pH 8.0 for at least 1 h; no other Bacillus AHL lactonase has been found to be stable under these conditions. AiiA(AI96) resists digestion by proteases and carp intestinal juice, and it has broad-spectrum substrate specificity. The supplementation of AiiA(AI96) into fish feed by oral administration significantly attenuated Aeromonas hydrophila infection in zebrafish. This is the first report of the oral administration of an AHL lactonase for the efficient control of A. hydrophila.
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