MomL, a novel marine-derived N-acyl homoserine lactonase from Muricauda olearia.
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):774-82. doi: 10.1128/AEM.02805-14. Epub
2014 Nov 14.MomL, a novel marine-derived N-acyl homoserine lactonase from Muricauda olearia.1, 1, 2, 1, 1, 1, 2, 3.1College of Marine Life Sciences, Ocean University of China, Qingdao, China.2Laboratory of Pharmaceutical Microbiology, Ghent University, Ghent, Belgium.3College of Marine Life Sciences, Ocean University of China, Qingdao, China xhzhang@.AbstractGram-negative bacteria use N-acyl homoserine lactones (AHLs) as quorum sensing (QS) signaling molecules for interspecies communication, and AHL-dependent QS is related with virulence factor production in many bacterial pathogens. Quorum quenching, the enzymatic degradation of the signaling molecule, would attenuate virulence rather than kill the pathogens, and thereby reduce the potential for evolution of drug resistance. In a previous study, we showed that Muricauda olearia Th120, belonging to the class Flavobacteriia, has strong AHL degradative activity. In this study, an AHL lactonase (designated MomL), which could degrade both short- and long-chain AHLs with or without a substitution of oxo-group at the C-3 position, was identified from Th120. Liquid chromatography-mass spectrometry analysis demonstrated that MomL functions as an AHL lactonase catalyzing AHL degradation through lactone hydrolysis. MomL is an AHL lactonase belonging to the metallo-β-lactamase superfamily that harbors an N-terminal signal peptide. The overall catalytic efficiency of MomL for C6-HSL is ~2.9 × 10(5) s(-1) M(-1). Metal analysis and site-directed mutagenesis showed that, compared to AiiA, MomL has a different metal-binding capability and requires the histidine and aspartic acid residues for activity, while it shares the "HXHXDH" motif with other AHL lactonases belonging to the metallo-β-lactamase superfamily. This suggests that MomL is a representative of a novel type of secretory AHL lactonase. Furthermore, MomL significantly attenuated the virulence of Pseudomonas aeruginosa in a Caenorhabditis elegans infection model, which suggests that MomL has the potential to be used as a therapeutic agent.PMID:
[Indexed for MEDLINE] Characterization of the AHL degradative activity of M. olearia Th120. AHL degradative activity of Th120 was analyzed by the A136 liquid X-Gal assay. AiiA and MB medium were used as the positive and negative controls, respectively. WC, S, CC, NC, negative control. In consideration of incomplete degradation of proteins, no proteinase K-treated WC was included. Four arabic numbers represent different pretreatments of each sample: untreated (row 1), recovery of AHLs by acidification (row 2), heat treated (row 3), and proteinase K treated (row 4).Appl Environ Microbiol. ):774-782.Multiple-sequence alignment of amino acid sequences of MomL, putative homologues, and other representative AHL lactonases. Sequence alignment was performed by the MUSCLE program in the MEGA software package and enhanced by ESPript 3.0. MomL homologue from Eudoraea adriatica (WP_) showed highest score when BLASTP searching nonredundant (NR) databases. Other sequences of AHL lactonase are AiiA from Bacillus sp. strain 240B1 (AAF62398), AidC from Chryseobacterium sp. strain StRB126 (BAM28988), QlcA from unculturable soil bacteria, and AttM (AAD43990) and AiiB (NP 396590) from Agrobacterium fabrum C58. These lactonases share the “HXHXDH” motif. MomL harbors an N-terminal signal peptide, and the predicted cleavage site was labeled by arrow. Empty circles indicate the conserved two Phe residues in some lactonases. Filled triangles show the amino acid residues chosen for site-directed mutagenesis.Appl Environ Microbiol. ):774-782.PAGE analysis of expressed MomL lacking the signal peptide sequence. MomL protein bands stained by Coomassie brilliant blue are indicated by arrows. (A) SDS-PAGE analysis of MomL-6×His-tagged protein. M, mo lane 1, insoluble fraction of induced E. coli BL21(DE3)/pET 24a(+)-momL(-SP); lane 2, lane 3, soluble fraction after passage over NTA-N lanes 4 and 5, 20 mM lanes 6, 7, and 8, 250 mM imidazole elution. (B) SDS-PAGE analysis of the purified MomL protein without signal peptide from E. coli BL21(DE3)/pTWIN1-momL(-SP). (C) In-gel QQ activity assay of the purified MomL protein from E. coli BL21(DE3)/pTWIN1-momL(-SP).Appl Environ Microbiol. ):774-782.LC-MS analysis of the MomL-hydrolyzed C6-HSL product. (A) LC profile of the MomL-hydrolyzed C6-HSL product. (B and C) ESI-MS analysis of LC fractions containing the 1.58-min product (B) and 1.71-min undigested C6-HSL (C).Appl Environ Microbiol. ):774-782.Physical and chemical parameters that affect MomL activity. The optimal temperature (A), temperature stability (B), and pH stability (C) of MomL activity and the effects of metal ions on MomL activity (D) were determined. The data were shown as means ± the standard deviation (SD).Appl Environ Microbiol. ):774-782.Effect of MomL on virulence factor production. The extracellular protease activity (A) and pyocyanin production (B) of P. aeruginosa PAO1 and C. elegans survival (C) were determined. NC, negative control. The data are shown as means ± the SD. One-way analysis of variance, followed by Dunnett's multiple-comparison test (GraphPad Prism v5.01), was performed to detect significant differences among treated groups and controls (***, P & 0.001; **, P & 0.01; *, P & 0.05).Appl Environ Microbiol. ):774-782.Neighbor-joining tree of AHL lactonases belonging to the metallo-β-lactamase superfamily based on amino acid sequences. Each of these AHL lactonases was experimentally identified, except the proteins designated with GenBank accession numbers. The dendrogram was constructed by neighbor-joining method with the MUSCLE program in the MEGA software package (1,000 bootstrap replicates). Bootstrap coefficients below 50% were not shown. Scale bar, 0.1 substitutions per amino acid position.Appl Environ Microbiol. ):774-782.Publication typeMeSH termsSubstancesSecondary source IDFull Text Sources
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