homoserine/cárie dentária

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Acyl homoserine lactone-mediated quorum sensing in the oral cavity: a paradigm revisited

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Acyl homoserine lactones (AHLs), the quorum sensing (QS) signals produced by Gram-negative bacteria, are currently considered to play a minor role in the development of oral biofilm since their production by oral pathogens has not been ascertained thus far. However, we report the presence of AHLs in

An eco-friendly sensor based on CQD@MIPs for detection of N-acylated homoserine lactones and its 3D printing applications

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N-acylated homoserine lactones (AHLs), a class of auto-inducers produced by Gram-negative bacteria, are typical signaling molecules in quorum sensing (QS) systems. Importantly, AHLs play a key role in determining the virulence of foodborne pathogens and reflect the activity of spoilage bacteria. In

A class-specific artificial receptor-based on molecularly imprinted polymer-coated quantum dot centers for the detection of signaling molecules, N-acyl-homoserine lactones present in gram-negative bacteria.

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Herein, a novel class-specific artificial receptor-based on molecularly imprinted polymer (MIP)-coated quantum dots (QDs@MIP) was synthesized, characterized, and used for the detection and quantification of the bacterial quorum signaling molecules N-acyl-homoserine lactones (AHLs), a class of

Unusual multiple production of N-acylhomoserine lactones a by Burkholderia sp. strain C10B isolated from dentine caries.

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Bacteria realize the ability to communicate by production of quorum sensing (QS) molecules called autoinducers, which regulate the physiological activities in their ecological niches. The oral cavity could be a potential area for the presence of QS bacteria. In this study, we report the isolation of

PA-I lectin from Pseudomonas aeruginosa binds acyl homoserine lactones.

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The study analyses the binding affinities of Pseudomonas aeruginosa PA-I lectin (PA-IL) to three N-acyl homoserine lactones (AHSL), quorum sensing signal molecules responsible for cell-cell communication in bacteria. It shows that like some plant lectins, PA-IL has a dual function and, besides its

Synthesis and biological evaluation of homoserine lactone derived ureas as antagonists of bacterial quorum sensing.

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A series of 15 racemic alkyl- and aryl-N-substituted ureas, derived from homoserine lactone, were synthesized and tested for their ability to competitively inhibit the action of 3-oxohexanoyl-l-homoserine lactone, the natural inducer of bioluminescence in the bacterium Vibrio fischeri. N-alkyl ureas

The effect of conformational variability of phosphotriesterase upon N-acyl-L-homoserine lactone and paraoxon binding: insights from molecular dynamics studies.

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The organophosphorous hydrolase (PTE) from Brevundimonas diminuta is capable of degrading extremely toxic organophosphorous compounds with a high catalytic turnover and broad substrate specificity. Although the natural substrate for PTE is unknown, its loop remodeling (loop 7-2/H254R) led to the

N-acyl homoserine lactone production by Klebsiella pneumoniae isolated from human tongue surface.

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Bacteria communicate by producing quorum sensing molecules called autoinducers, which include autoinducer-1, an N-hexanoyl homoserine lactone (AHL), and autoinducer-2. Bacteria present in the human oral cavity have been shown to produce autoinducer-2, but not AHL. Here, we report the isolation of

Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily.

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BACKGROUND Homoserine kinase (HSK) catalyzes an important step in the threonine biosynthesis pathway. It belongs to a large yet unique class of small metabolite kinases, the GHMP kinase superfamily. Members in the GHMP superfamily participate in several essential metabolic pathways, such as amino

N-acyl homoserine lactone-producing Pseudomonas putida strain T2-2 from human tongue surface.

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Bacterial cell-to-cell communication (quorum sensing) refers to the regulation of bacterial gene expression in response to changes in microbial population density. Quorum sensing bacteria produce, release and respond to chemical signal molecules called autoinducers. Bacteria use two types of

Tailor-made LasR agonists modulate quorum sensing in Pseudomonas aeruginosa.

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The primary quorum sensing system in the opportunistic pathogen Pseudomonas aeruginosa is regulated through the synthesis and secretion of N-3-oxo-dodecanoyl-L-homoserine lactone (C12) which binds the transcriptional activator LasR. In this study we report the design, synthesis and biological

Crystal structure of the N-terminal domain of VqsR from Pseudomonas aeruginosa at 2.1 Å resolution.

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VqsR is a quorum-sensing (QS) transcriptional regulator which controls QS systems (las, rhl and pqs) by directly downregulating the expression of qscR in Pseudomonas aeruginosa. As a member of the LuxR family of proteins, VqsR shares the common motif of a helix-turn-helix (HTH)-type DNA-binding

A novel compound to maintain a healthy oral plaque ecology in vitro.

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OBJECTIVE Dental caries is caused by prolonged episodes of low pH due to acid production by oral biofilms. Bacteria within such biofilms communicate via quorum sensing (QS). QS regulates several phenotypic biofilm parameters, such as biofilm formation and the production of virulence factors. In this

Structural Insights into Substrate Specificity of Cystathionine γ-Synthase from Corynebacterium glutamicum.

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Cystathionine γ-synthase (MetB) condenses O-acetyl-l-homoserine (OAHS) or O-succinyl-l-homoserine (OSHS) with cysteine to produce cystathionine. To investigate the molecular mechanisms and substrate specificity of MetB from Corynebacterium glutamicum (CgMetB), we determined its crystal structure at

A phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-γ-lactonase from Bacillus thuringiensis.

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Autoinducer inactivator A (AiiA) is a metal-dependent N-acyl homoserine lactone hydrolase that displays broad substrate specificity but shows a preference for substrates with long N-acyl substitutions. Previously, crystal structures of AiiA in complex with the ring-opened product

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