z-logo
open-access-imgOpen Access
Identification and Characterization ofN-Acylhomoserine Lactone-Acylase from the Fish IntestinalShewanellasp. Strain MIB015
Author(s) -
Tomohiro Morohoshi,
Shigehisa Nakazawa,
Atsushi Ebata,
Norihiro Kato,
Tsukasa Ikeda
Publication year - 2008
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.80139
Subject(s) - quorum sensing , vibrio anguillarum , shewanella , quorum quenching , shewanella oneidensis , biofilm , microbiology and biotechnology , strain (injury) , escherichia coli , biology , bacteria , chemistry , gene , vibrio , biochemistry , genetics , anatomy
N-Acylhomoserine lactones (AHLs) are used as quorum-sensing signal molecules by many gram-negative bacteria. We have reported that Shewanella sp. strain MIB015 degrades AHLs. In the present study, we cloned the aac gene from MIB015 by PCR with specific primers based on the aac gene in Shewanella oneidensis strain MR-1, which showed high homology with the known AHL-acylases. Escherichia coli expressing Aac showed high degrading activity of AHLs with long acyl chains. HPLC analysis revealed that Aac worked as AHL-acylase, which hydrolyzed the amide bond of AHL. In addition, expression of Aac in fish pathogen Vibrio anguillarum markedly reduced AHL production and biofilm formation. In conclusion, this study indicates that Aac might be effective in quenching quorum sensing of fish pathogens.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom