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Title 

Identification of extracellular N-acylhomoserine lactone acylase from a Streptomyces sp. and its application to quorum quenching

Authors 

Sun Yang ParkHye Ok KangH S JangJung-Kee LeeB T KooD Y Yum

Publisher 

American Society for Microbiology

Issue Date 

2005

Citation 

Applied and Environmental Microbiology, vol. 71, no. 5, pp. 2632-2641

Keywords 

antibioticsbacteriamass spectrometrylactonepathogenic bacteriasoil bacteriavirulence factorsenzymesamidaseantiinfective agent

Abstract 

N-Acylhomoserine lactones (AHLs) play an important role in regulating virulence factors in pathogenic bacteria. Recently, the enzymatic inactivation of AHLs, which can be used as antibacterial targets, has been identified in several soil bacteria. In this study, strain M664, identified as a Streptomyces sp., was found to secrete an AHL-degrading enzyme into a culture medium. The ahlM gene for AHL degradation from Streptomyces sp. strain M664 was cloned, expressed heterologously in Streptomyces lividans, and purified. The enzyme was found to be a heterodimeric protein with subunits of approximately 60 kDa and 23 kDa. A comparison of AhlM with known AHL-acylases, Ralstonia strain XJ12B AiiD and Pseudomonas aeruginosa PAO1 PvdQ, revealed 35% and 32% identities in the deduced amino acid sequences, respectively. However, AhlM was most similar to the cyclic lipopeptide acylase from Streptomyces sp. strain FERM BP-5809, exhibiting 93% identity. A mass spectrometry analysis demonstrated that AhlM hydrolyzed the amide bond of AHL, releasing homoserine lactone. AhlM exhibited a higher deacylation activity toward AHLs with long acyl chains rather than short acyl chains. Interestingly, AhlM was also found to be capable of degrading penicillin G by deacylation, showing that AhlM has a broad substrate specificity. The addition of AhlM to the growth medium reduced the accumulation of AHLs and decreased the production of virulence factors, including elastase, total protease, and LasA, in P. aeruginosa. Accordingly, these results suggest that AHL-acylase, AhlM could be effectively applied to the control of AHL-mediated pathogenicity.

ISSN 

0099-2240

Link 

http://dx.doi.org/10.1128/AEM.71.5.2632-2641.2005

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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