Orally Administered Thermostable
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            -Acyl Homoserine Lactonase from Bacillus sp. Strain AI96 Attenuates Aeromonas hydrophila Infection in Zebrafish

Cao, Yanan; He, Shunping; Zhou, Zhigang; MeiChao, Zhang; Mao, Wenfei; Zhang, Huitu; Yao, Bin

doi:10.1128/aem.06139-11

Cited by 125 publications

(125 citation statements)

References 53 publications

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“…AiiA N26.2 protein can be stored at 4°C for up to 5 days or at 20°C for up to 3 days, maintaining its activity at least 80 % of the maximal level. Our results are consistent with those reported by other authors [12,18,19]. These properties of AiiA N26.2 protein can facilitate its future oral administration via supplementation into fish/shrimp feed ingredients for efficient control of QS-regulated aquaculture pathogens.…”

Section: Discussionsupporting

confidence: 83%

In Vitro Characterization of a Recombinant AHL-Lactonase from Bacillus cereus Isolated from a Striped Catfish (Pangasianodon hypophthalmus) Pond

Tình

Dung²,

Trung³

et al. 2013

Indian J Microbiol

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aiiA gene encoding AHL-lactonase was isolated from Bacillus cereus strain N26.2, originating from a striped catfish (Pangasianodon hypophthalmus) pond in Vietnam. This gene, abbreviated as aiiA(N26.2), was cloned and expressed in a competent Escherichia coli strain BL21(DE3)pLysS. The resulting protein, abbreviated as AiiA N26.2 , was highly active in the pH range of 6-8 and could retain 80 % of the maximum activity under storage for 5 days at 4°C or for 3 days at 20°C. These properties of AiiA N26.2 protein confers its future application via feed supplementation, with the purpose of controlling aquaculture pathogens which regulate the virulence via a quorum sensing system.

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Section: Discussionsupporting

confidence: 83%

In Vitro Characterization of a Recombinant AHL-Lactonase from Bacillus cereus Isolated from a Striped Catfish (Pangasianodon hypophthalmus) Pond

Tình

Dung²,

Trung³

et al. 2013

Indian J Microbiol

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“…Furthermore, in other reports, the administration of purified QQ enzyme to animals showed a similar effect. Oral administration of purified AiiA AI96 protein protected zebrafish from killing by Aeromonas hydrophila (39). Likewise, coinjection of AiiA B546 with A. hydrophila decreased the mortality rate in common carp (40), and exogenous addition of PvdQ protein in rearing medium attenuated the virulence of P. aeruginosa PAO1 to C. elegans (41).…”

Section: Moml Represents a Novel Class Of Extracellular Ahl Lactonasesmentioning

confidence: 98%

MomL, a Novel Marine-Derived N -Acyl Homoserine Lactonase from Muricauda olearia

Tang

Brackman

et al. 2015

Appl Environ Microbiol

112

129

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bGram-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-␤-lactamase superfamily that harbors an N-terminal signal peptide. The overall catalytic efficiency of MomL for C 6 -HSL is ϳ2.9 ؋ 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-␤-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. N-Acyl homoserine lactones (AHLs) are quorum-sensing (QS) signaling molecules that are used by many Gram-negative bacteria to communicate within species, to regulate gene expression and to synchronize social behaviors, such as biofilm formation, bioluminescence, and secretion of virulence factors (1, 2). An AHL molecule typically consists of a homoserine lactone and an acyl chain with an even number of carbons, with an occasional modification (hydroxy or olefinic double bond) at the C-3 position (1). It has been well established that AHL-dependent QS regulates virulence factor production in many bacterial pathogens, such as Pseudomonas aeruginosa, Erwinia carotovora, Vibrio spp., and Burkholderia spp. (1). Interference with QS has been recognized as a promising antivirulence therapy. Disturbing the QS systems in these pathogens would attenuate virulence rather than kill the bacteria and thereby weaken the selective pressure imposed on the pathogens and reduce the potential for evolution of drug resistance (3). QS inhibitors (QSIs; small molecules) and quorum-quenching (QQ) enzymes can both be used to interfere with QS. QSIs generally act to inactivate autoinducer synthases or receptors through competitive binding, whereas QQ enzymes switch off signal transmission through degradation of the signaling molecules. It has been demonstrated th...

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“…(reviewed by Tinh et al 2008;Cao et al 2012). Thus, the identification of biological functions in marine microorganisms could have wide-reaching applications.…”

Section: Enzymes That Degrade Biofilm-forming Qs Signalsmentioning

confidence: 99%

Mini-review: Inhibition of biofouling by marine microorganisms

2013

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Any natural or artificial substratum exposed to seawater is quickly fouled by marine microorganisms and later by macrofouling species. Microfouling organisms on the surface of a substratum form heterogenic biofilms, which are composed of multiple species of heterotrophic bacteria, cyanobacteria, diatoms, protozoa and fungi. Biofilms on artificial structures create serious problems for industries worldwide, with effects including an increase in drag force and metal corrosion as well as a reduction in heat transfer efficiency. Additionally, microorganisms produce chemical compounds that may induce or inhibit settlement and growth of other fouling organisms. Since the last review by the first author on inhibition of biofouling by marine microbes in 2006, significant progress has been made in the field. Several antimicrobial, antialgal and antilarval compounds have been isolated from heterotrophic marine bacteria, cyanobacteria and fungi. Some of these compounds have multiple bioactivities. Microorganisms are able to disrupt biofilms by inhibition of bacterial signalling and production of enzymes that degrade bacterial signals and polymers. Epibiotic microorganisms associated with marine algae and invertebrates have a high antifouling (AF) potential, which can be used to solve biofouling problems in industry. However, more information about the production of AF compounds by marine microorganisms in situ and their mechanisms of action needs to be obtained. This review focuses on the AF activity of marine heterotrophic bacteria, cyanobacteria and fungi and covers publications from 2006 up to the end of 2012.

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Orally Administered Thermostable N -Acyl Homoserine Lactonase from Bacillus sp. Strain AI96 Attenuates Aeromonas hydrophila Infection in Zebrafish

Cited by 125 publications

References 53 publications

In Vitro Characterization of a Recombinant AHL-Lactonase from Bacillus cereus Isolated from a Striped Catfish (Pangasianodon hypophthalmus) Pond

In Vitro Characterization of a Recombinant AHL-Lactonase from Bacillus cereus Isolated from a Striped Catfish (Pangasianodon hypophthalmus) Pond

MomL, a Novel Marine-Derived N -Acyl Homoserine Lactonase from Muricauda olearia

Mini-review: Inhibition of biofouling by marine microorganisms

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