Detection of Quorum Sensing System (Cell to Cell Communication) Using  Marker Strains in Vibrio alginolyticus Strains and Determine Virulence under  Master of this System

Filik, Nurdan; Kubilay, Ayşegül

doi:10.12681/jhvms.28525

Cited by 2 publications

(1 citation statement)

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“…Afterward, the supernatant was transferred to a new centrifuge tube to extract the concentrated organic fraction, and deionized water and moss black phenol were added and incubated at 80 • C for 30 min. After cooling, the absorbance was measured at 421 nm [64,65]. The test was performed in triplicates.…”

Section: Elastase Assay and Rhamnolipid Assaymentioning

confidence: 99%

Discovery of Melittin as Triple-Action Agent: Broad-Spectrum Antibacterial, Anti-Biofilm, and Potential Anti-Quorum Sensing Activities

Yang,

Ma,

Chen

et al. 2024

Molecules

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The development of antibiotic-resistant microorganisms is a major global health concern. Recently, there has been an increasing interest in antimicrobial peptides as a therapeutic option. This study aimed to evaluate the triple-action (broad-spectrum antibacterial, anti-biofilm, and anti-quorum sensing activities) of melittin, a membrane-active peptide present in bee venom. The minimum inhibitory concentration and minimum bactericidal concentration of the melittin were determined using the microdilution method and agar plate counting. Growth curve analysis revealed that melittin showed a concentration-dependent antibacterial activity. Scanning electron microscope analysis revealed that melittin treatment altered the morphology. Confocal laser scanning microscope revealed that melittin increased the membrane permeability and intracellular ROS generation in bacteria, all of which contribute to bacterial cell death. In addition, the crystal violet (CV) assay was used to test the anti-biofilm activity. The CV assay demonstrated that melittin inhibited biofilm formation and eradicated mature biofilms. Biofilm formation mediated by quorum sensing (QS) plays a major role in this regard, so molecular docking and molecular dynamics analysis confirmed that melittin interacts with LasR receptors through hydrogen bonds, and further evaluates the anti-QS activity of melittin through the production of virulence factors (pyocyanin, elastase, and rhamnolipid), exopolysaccharides secretion, and bacterial motility, that may be the key to inhibiting the biofilm formation mechanism. The present findings highlight the promising role of melittin as a broad-spectrum antibacterial, anti-biofilm agent, and potential QS inhibitor, providing a new perspective and theoretical basis for the development of alternative antibiotics.

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Section: Elastase Assay and Rhamnolipid Assaymentioning

confidence: 99%