AidP, a novel N-Acyl homoserine lactonase gene from Antarctic Planococcus sp.

See-Too, Wah-Seng; Ee, Robson; Lim, Yan-Lue; Convey, Peter; Pearce, David A.; Yin, Wai‐Fong; Chan, Kok‐Gan

doi:10.1038/srep42968

Cited by 18 publications

(18 citation statements)

References 46 publications

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“…The enzyme assays have confirmed that the AiiK was capable of degrading AHLs, including C 6 -HSL, N-(3-oxohexanoyl)-L-homoserine lactone (3-Oxo-C 6 -HSL), N-decanoyl-L-homoserine lactone (C 10 -HSL), and N-tetradecanoyl-L-homoserine lactone (C 14 -HSL) (data not shown). The opened lactone ring of AHL, which was catalyzed by AHL lactonase, was acidified at a low pH and the re-lactonization of the opened ring will be taken place resulting in an intact AHL 18 – 20 . Hydrolysis assay (Fig.…”

Section: Resultsmentioning

confidence: 99%

Characterization of AiiK, an AHL lactonase, from Kurthia huakui LAM0618T and its application in quorum quenching on Pseudomonas aeruginosa PAO1

Dong

Zhu

Guo

et al. 2018

Sci Rep

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N-Acyl homoserine lactones (AHLs) act as the key quorum sensing (QS) signal molecules in gram-negative bacteria, which coordinates gene expression and then activates various processes, including biofilm formation and production of virulence factors in some pathogens. Quorum quenching (QQ), which is the inactivation of the signal molecules by means of enzymatic degradation or modification, inhibits the processes of QS rather than killing the pathogens and is a promising antipathogenic strategy to control the bacterial pathogens. In this study, an AHL lactonase gene (named aiiK) was cloned from Kurthia huakuii LAM0618T and the AHL lactonase AiiK was expressed by Escherichia coli. AiiK exhibits a variable substrate spectrum and efficient degradation of the AHL compounds. The enzyme assays demonstrated that AiiK behaves as an AHL lactonase that can hydrolyze the lactone bond of the AHLs. The total hydrolytic efficiency of AiiK for C10-HSL is 3.9 s−1·mM−1. AiiK can also maintain 20% activity after 12 h incubation at 37 °C and demonstrate great resistance to α-chymotrypsin, trypsin, and protease K. Furthermore, AiiK significantly inhibits the biofilm formation and attenuates extracellular proteolytic activity and pyocyanin production of Pseudomonas aeruginosa PAO1, which indicates the potential application of AiiK as a biocontrol agent or an anti-pathogenic drug.

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Section: Resultsmentioning

confidence: 99%

Characterization of AiiK, an AHL lactonase, from Kurthia huakui LAM0618T and its application in quorum quenching on Pseudomonas aeruginosa PAO1

Dong

Zhu

Guo

et al. 2018

Sci Rep

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“…As suggested by Thomas et al (2005), completely conserved zinc-binding residues present in all known AHL lactonases are histidine 104, histidine 106, and histidine 169 in the metal site 1 and aspartic acid 108, histidine 109, and histidine 235 in the metal site 2 [39]. A mutagenic study of AiiA type lactonases highlighted the involvement of tyrosine (Y 194) and aspartic acid (D 108) residues in the catalytic mechanism [40]. The putative AHL acylase gene from Shewanella algae QQ5 was also amplified and sequenced.…”

Section: Discussionmentioning

confidence: 96%

Quorum Quenching Properties and Probiotic Potentials of Intestinal Associated Bacteria in Asian Sea Bass Lates calcarifer

et al. 2019

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Quorum quenching (QQ), the enzymatic degradation of N-acyl homoserine lactones (AHLs), has been suggested as a promising strategy to control bacterial diseases. In this study, 10 AHL-degrading bacteria isolated from the intestine of barramundi were identified by 16S rDNA sequencing. They were able to degrade both short and long-chain AHLs associated with several pathogenic Vibrio species (spp.) in fish, including N-[(RS)-3-Hydroxybutyryl]-l-homoserine lactone (3-oh-C4-HSL), N-Hexanoyl-l-homoserine lactone (C6-HSL), N-(β-Ketocaproyl)-l-homoserine lactone (3-oxo-C6-HSL), N-(3-Oxodecanoyl)-l-homoserine lactone (3-oxo-C10-HSL), N-(3-Oxotetradecanoyl)-l-homoserine lactone (3-oxo-C14-HSL). Five QQ isolates (QQIs) belonging to the Bacillus and Shewanella genera, showed high capacity to degrade both synthetic AHLs as well as natural AHLs produced by Vibrio harveyi and Vibrio alginolyticus using the well-diffusion method and thin-layer chromatography (TLC). The genes responsible for QQ activity, including aiiA, ytnP, and aaC were also detected. Analysis of the amino acid sequences from the predicted lactonases revealed the presence of the conserved motif HxHxDH. The selected isolates were further characterized in terms of their probiotic potentials in vitro. Based on our scoring system, Bacillus thuringiensis QQ1 and Bacillus cereus QQ2 exhibited suitable probiotic characteristics, including the production of spore and exoenzymes, resistance to bile salts and pH, high potential to adhere on mucus, appropriate growth abilities, safety to barramundi, and sensitivity to antibiotics. These isolates, therefore, constitute new QQ probiotics that could be used to control vibriosis in Lates calcalifer.

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“…Strain R3.8 was isolated using basal medium supplied with C 6 -HSL as sole carbon source. An isolation temperature of 4 °C was used to select for psychrophilic or psychrotolerant bacteria maintained on Luria Bertani (LB) agar [ 5 , 6 ]. The strain exhibited a 98.6% 16S rRNA nucleotide sequence similarity with 10.1601/nm.20084, the most phylogenetically closely related Arthrobacter species with standing in nomenclature (Fig.…”

Section: Organism Informationmentioning

confidence: 99%

Complete genome of Arthrobacter alpinus strain R3.8, bioremediation potential unraveled with genomic analysis

See-Too

Lim

et al. 2017

Stand in Genomic Sci

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Arthrobacter alpinus R3.8 is a psychrotolerant bacterial strain isolated from a soil sample obtained at Rothera Point, Adelaide Island, close to the Antarctic Peninsula. Strain R3.8 was sequenced in order to help discover potential cold active enzymes with biotechnological applications. Genome analysis identified various cold adaptation genes including some coding for anti-freeze proteins and cold-shock proteins, genes involved in bioremediation of xenobiotic compounds including naphthalene, and genes with chitinolytic and N-acetylglucosamine utilization properties and also plant-growth-influencing properties. In this genome report, we present a complete genome sequence of A. alpinus strain R3.8 and its annotation data, which will facilitate exploitation of potential novel cold-active enzymes.Electronic supplementary materialThe online version of this article (doi:10.1186/s40793-017-0264-0) contains supplementary material, which is available to authorized users.

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AidP, a novel N-Acyl homoserine lactonase gene from Antarctic Planococcus sp.

Cited by 18 publications

References 46 publications

Characterization of AiiK, an AHL lactonase, from Kurthia huakui LAM0618T and its application in quorum quenching on Pseudomonas aeruginosa PAO1

Characterization of AiiK, an AHL lactonase, from Kurthia huakui LAM0618T and its application in quorum quenching on Pseudomonas aeruginosa PAO1

Quorum Quenching Properties and Probiotic Potentials of Intestinal Associated Bacteria in Asian Sea Bass Lates calcarifer

Complete genome of Arthrobacter alpinus strain R3.8, bioremediation potential unraveled with genomic analysis

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