AmiE, a Novel
            <i>N</i>
            -Acylhomoserine Lactone Acylase Belonging to the Amidase Family, from the Activated-Sludge Isolate Acinetobacter sp. Strain Ooi24

Ochiai, Seiji; Yasumoto, Sera; Morohoshi, Toshio; Ikeda, Tsukasa

doi:10.1128/aem.02190-14

Cited by 39 publications

(20 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Interestingly, it has been recently described in vitro that Acinetobacter sp. strain Ooi24 expresses an N -acylhomoserine lactone acylase belonging to the amidase family (named also AmiE in this bacterium) that degrades specifically 3-oxo-C 12 -HSL compound40 suggesting that P. aeruginosa AmiE could directly degrade this QS signal. However, so far, no acylase activity could be assigned to P. aeruginosa AmiE.…”

Section: Discussionmentioning

confidence: 99%

The aliphatic amidase AmiE is involved in regulation of Pseudomonas aeruginosa virulence

Clamens

Rosay

Crépin

et al. 2017

Sci Rep

View full text Add to dashboard Cite

We have previously shown that the eukaryotic C-type natriuretic peptide hormone (CNP) regulates Pseudomonas aeruginosa virulence and biofilm formation after binding on the AmiC sensor, triggering the amiE transcription. Herein, the involvement of the aliphatic amidase AmiE in P. aeruginosa virulence regulation has been investigated. The proteome analysis of an AmiE over-producing strain (AmiE+) revealed an expression change for 138 proteins, including some that are involved in motility, synthesis of quorum sensing compounds and virulence regulation. We observed that the AmiE+ strain produced less biofilm compared to the wild type, and over-produced rhamnolipids. In the same line, AmiE is involved in P. aeruginosa motilities (swarming and twitching) and production of the quorum sensing molecules N-acyl homoserine lactones and Pseudomonas Quinolone Signal (PQS). We observed that AmiE overproduction reduced levels of HCN and pyocyanin causing a decreased virulence in different hosts (i.e. Dictyostelium discoideum and Caenorhabditis elegans). This phenotype was further confirmed in a mouse model of acute lung infection, in which AmiE overproduction resulted in an almost fully virulence decrease. Taken together, our data suggest that, in addition to its role in bacterial secondary metabolism, AmiE is involved in P. aeruginosa virulence regulation by modulating pilus synthesis and cell-to-cell communication.

show abstract

Section: Discussionmentioning

confidence: 99%

The aliphatic amidase AmiE is involved in regulation of Pseudomonas aeruginosa virulence

Clamens

Rosay

Crépin

et al. 2017

Sci Rep

View full text Add to dashboard Cite

show abstract

“…Acylases active on AHLs have been observed to vary in their substrate specificities, and separate into different phylogenetic clusters (Ochiai et al 2014). Enzymes of the AAC group (including AAC from Shewanella sp., PvdQ from P. aeruginosa, AhlM from Streptomyces sp.…”

Section: Discussionmentioning

confidence: 99%

“…group can act on both long and short chain AHLs. A newly characterized AHL acylase AmiE of the amidase family (Ochiai et al 2014) possesses an activity preference for long chain unsubstituted AHLs similar to PVAs. However, the PVA enzymes shared little sequence similarity (<15%) with any of the known acylases active on AHLs (Fig.…”

Section: Discussionmentioning

confidence: 99%

Penicillin V acylases from gram-negative bacteria degrade N-acylhomoserine lactones and attenuate virulence in Pseudomonas aeruginosa

Sunder

Utari

Ramasamy

et al. 2016

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Virulence pathways in gram-negative pathogenic bacteria are regulated by quorum sensing mechanisms, through the production and sensing of N-acylhomoserine lactone (AHL) signal molecules. Enzymatic degradation of AHLs leading to attenuation of virulence (quorum quenching) could pave the way for the development of new antibacterials. Penicillin V acylases (PVAs) belong to the Ntn hydrolase superfamily, together with AHL acylases. PVAs are exploited widely in the pharmaceutical industry, but their role in the natural physiology of their native microbes is not clearly understood. This report details the characterization of AHL degradation activity by homotetrameric PVAs from two gram-negative plant pathogenic bacteria, Pectobacterium atrosepticum (PaPVA) and Agrobacterium tumefaciens (AtPVA). Both the PVAs exhibited substrate specificity for degrading long-chain AHLs. Exogenous addition of these enzymes into Pseudomonas aeruginosa greatly diminished the production of elastase and pyocyanin and biofilm formation and increased the survival rate in an insect model of acute infection. Subtle structural differences in the PVA active site that regulate specificity for acyl chain length have been characterized, which could reflect the evolution of AHL-degrading acylases in relation to the environment of the bacteria that produce them and also provide strategies for enzyme engineering. The potential for using these enzymes as therapeutic agents in clinical applications and a few ideas about their possible significance in microbial physiology have also been discussed.

show abstract

“…In addition to penicillin acylase, an aliphatic amidase AmiE (EC. 3.5.1.4) was found in the genome of Az39 (fig 192.31.peg.3259) and both enzymes have been described as AHL-acylases in some databases and literature (Ochiai et al 2014). Results found through BRENDA (http://www.brenda-enzymes.org) depended on the organism studied.…”

Section: Quorum Quenchingmentioning

confidence: 99%

Azospirillum brasilenseAz39, a model rhizobacterium withAHLquorum‐quenchingcapacity

et al. 2019

View full text Add to dashboard Cite

Aims The aim of this research was to analyse the quorum‐sensing (QS) and quorum‐quenching (QQ) mechanisms based on N‐acyl‐l‐homoserine lactones (AHLs) in Azospirillum brasilense Az39, a strain with remarkable capacity to benefit a wide range of crops under agronomic conditions. Methods and results We performed an in silico and in vitro analysis of the quorum mechanisms in A. brasilense Az39. The results obtained in vitro using the reporter strains Chromobacterium violaceum and Agrobacterium tumefaciens and liquid chromatography coupled with mass‐mass spectrometry analysis showed that although Az39 does not produce AHL molecules, it is capable of degrading them by at least two hypothetical enzymes identified by bioinformatics approach, associated with the bacterial cell. In Az39 cultures supplemented with 500 nmol l−1 of the C3 unsubstituted AHLs (C4, C6, C8, C10, C12, C14), AHL levels were lower than in noninoculated LB media controls. Similar results were observed upon the addition of AHLs with hydroxy (OH‐) and keto (oxo‐) substitutions in C3. These results not only demonstrate the ability of Az39 to degrade AHLs. They also show the wide spectrum of molecules that can be degraded by this bacterium. Conclusions Although A. brasilense Az39 is a silent bacterium unable to produce AHL signals, it is able to interrupt the communications between other bacteria and/or plants by a QQ activity. Significance and Impact of the Study This is the first report confirming by unequivocal methodology the ability of A. brasilense, one of the most agriculturally used benefic bacteria around the world, to degrade AHLs by a QQ mechanism.

show abstract

AmiE, a Novel N -Acylhomoserine Lactone Acylase Belonging to the Amidase Family, from the Activated-Sludge Isolate Acinetobacter sp. Strain Ooi24

Cited by 39 publications

References 35 publications

The aliphatic amidase AmiE is involved in regulation of Pseudomonas aeruginosa virulence

The aliphatic amidase AmiE is involved in regulation of Pseudomonas aeruginosa virulence

Penicillin V acylases from gram-negative bacteria degrade N-acylhomoserine lactones and attenuate virulence in Pseudomonas aeruginosa

Azospirillum brasilenseAz39, a model rhizobacterium withAHLquorum‐quenchingcapacity

Contact Info

Product

Resources

About