scholarly journals Labrenzia sp. BM1: A Quorum Quenching Bacterium That Degrades N-acyl Homoserine Lactones via Lactonase Activity

Sensors ◽  
2014 ◽  
Vol 14 (7) ◽  
pp. 11760-11769 ◽  
Author(s):  
Norshazliza Ghani ◽  
Siti Norizan ◽  
Xin Chan ◽  
Wai-Fong Yin ◽  
Kok-Gan Chan
Keyword(s):  
Quorum Quenching ◽  
Homoserine Lactones ◽  
Acyl Homoserine Lactones

scholarly journals Insights from the Genome Sequence of Quorum-Quenching Staphylococcus sp. Strain AL1, Isolated from Traditional Chinese Soy Sauce Brine Fermentation

2012 ◽  
Vol 194 (23) ◽  
pp. 6611-6612 ◽  
Author(s):  
Teik-Min Chong ◽  
Hun-Jiat Tung ◽  
Wai-Fong Yin ◽  
Kok-Gan Chan
Keyword(s):  
Quorum Sensing ◽  
Genome Sequence ◽  
Draft Genome ◽  
Quorum Quenching ◽  
Soy Sauce ◽  
Whole Genome Sequence ◽  
Whole Genome ◽  
Content Type ◽  
Homoserine Lactones ◽  
Acyl Homoserine Lactones

ABSTRACTWe report the draft genome sequence ofStaphylococcussp. strain AL1, which degrades quorum-sensing molecules (namely,N-acyl homoserine lactones). To the best of our knowledge, this is the first documentation that reports the whole genome sequence and quorum-quenching activity ofStaphylococcussp. strain AL1.

scholarly journals Haloperoxidase Mediated Quorum Quenching by Nitzschia cf pellucida: Study of the Metabolization of N-Acyl Homoserine Lactones by a Benthic Diatom

Marine Drugs ◽  
2014 ◽  
Vol 12 (1) ◽  
pp. 352-367 ◽  
Author(s):  
Michail Syrpas ◽  
Ewout Ruysbergh ◽  
Lander Blommaert ◽  
Bart Vanelslander ◽  
Koen Sabbe ◽  
...  
Keyword(s):  
Quorum Quenching ◽  
Benthic Diatom ◽  
Homoserine Lactones ◽  
Acyl Homoserine Lactones

scholarly journals Marine-Source Quorum Quenching Enzyme YtnP to Improve Hygiene Quality in Dental Units

Marine Drugs ◽  
2021 ◽  
Vol 19 (4) ◽  
pp. 225
Author(s):  
Xiaohui Sun ◽  
Philip Hill ◽  
Jia Liu ◽  
Jing Qian ◽  
Yuting Ma ◽  
...  
Keyword(s):  
Biofilm Formation ◽  
Quorum Quenching ◽  
Bacillus Velezensis ◽  
Antifouling Activity ◽  
Homoserine Lactones ◽  
Water Filter ◽  
E Coli ◽  
Acyl Homoserine Lactones ◽  
Dental Practitioners ◽  
Marine Source

Biofilm in dental unit water lines may pose a health risk to patients and dental practitioners. An AdiC-like quorum quenching enzyme, YtnP, was cloned from a deep-sea probiotic Bacillus velezensis, and heterologously expressed in E. coli to examine the application on the improvement of hygiene problems caused by biofilm infection of Pseudomonas aeruginosa in dental units. Pseudomonas bacteria were isolated from dental chair units and used to grow static biofilms in the laboratory. A water filter system was designed to test the antifouling activity of YtnP in Laboratory, to simulate the biofilm contamination on water filter in dental unit water lines. The results demonstrated that the enzyme of YtnP was able to degrade the N-acyl homoserine lactones, significantly inhibited the EPS generation, biofilm formation, and virulence factors production (pyocyanin and rhamnolipid) of P. aeruginosa, and was efficient on the antifouling against P. aeruginosa. The findings in this study indicated the possibility of YtnP as novel disinfectant reagent for hygiene treatment in dental units.

scholarly journals Hybrid Assembly of the Quorum-Quenching Isolate Variovorax paradoxus VAI-C Genome Sequence

2021 ◽  
Vol 10 (19) ◽  
Author(s):  
Christopher J. Ne Ville ◽  
Jared R. Leadbetter ◽  
Paul M. Orwin
Keyword(s):  
Genome Sequence ◽  
Quorum Quenching ◽  
Sole Source ◽  
Hybrid Assembly ◽  
Content Type ◽  
Homoserine Lactones ◽  
Variovorax Paradoxus ◽  
Acyl Homoserine Lactones ◽  
C Genome

ABSTRACT Variovorax paradoxus VAI-C was isolated due to its ability to utilize acyl-homoserine lactones (AHLs) as the sole source of carbon, energy, and nitrogen. Here, we present a hybrid assembly of the V. paradoxus VAI-C genome sequence, consisting of a primary chromosome, a secondary chromid, and a plasmid.

scholarly journals Human Paraoxonase-2 (PON2): Protein Functions and Modulation

Antioxidants ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 256
Author(s):  
Giuseppe Manco ◽  
Elena Porzio ◽  
Teresa Maria Carusone
Keyword(s):  
Hydrolytic Activity ◽  
Principal Function ◽  
Substrate Specificities ◽  
Homoserine Lactones ◽  
Stress Control ◽  
Acyl Homoserine Lactones ◽  
Bacterial Quorum Sensing ◽  
Protein Functions ◽  
Bacterial Quorum ◽  
Hydrolyzing Enzymes

PON1, PON2, and PON3 belong to a family of lactone hydrolyzing enzymes endowed with various substrate specificities. Among PONs, PON2 shows the highest hydrolytic activity toward many acyl-homoserine lactones (acyl-HL) involved in bacterial quorum-sensing signaling. Accordingly, defense against pathogens, such as Brevundimonas aeruginosa (B. aeruginosa), was postulated to be the principal function of PON2. However, recent findings have highlighted the importance of PON2 in oxidative stress control, inhibition of apoptosis, and the progression of various types of malignancies. This review focuses on all of these aspects of PON2.

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