Identification of Quorum Quenching N-Acyl Homoserine Lactonases from Priestia aryabhattai J1D and Bacillus cereus G Isolated from the Rhizosphere.

Autor: Shevate SN; Department of Microbiology, MES Abasaheb Garware College Affiliated to Savitribai Phule Pune University, Pune, Maharashtra, India., Shinde SS; Annasaheb Kulkarni Department of Biodiversity MES Abasaheb Garware College Affiliated to Savitribai Phule Pune University, Pune, Maharashtra, India., Bankar AV; Department of Microbiology, MES Abasaheb Garware College Affiliated to Savitribai Phule Pune University, Pune, Maharashtra, India., Patil NP; Department of Microbiology, MES Abasaheb Garware College Affiliated to Savitribai Phule Pune University, Pune, Maharashtra, India. niranjan75@gmail.com.
Jazyk: angličtina
Zdroj: Current microbiology [Curr Microbiol] 2023 Jan 30; Vol. 80 (3), pp. 86. Date of Electronic Publication: 2023 Jan 30.
DOI: 10.1007/s00284-023-03186-3
Abstrakt: Several pathogenic bacteria communicate using N-acyl homoserine lactone (AHL) as a quorum sensing (QS) molecule. The process of interfering with the QS system is known as quorum quenching (QQ), it is an effective tool to control QS-dependent virulence in pathogens. In the present study, rhizosphere bacterial isolates were screened for their ability to produce AHL lactonase enzyme as QQ molecules, which hydrolyses AHL signalling molecules and consequently blocks the QS system. Potent N-hexanoyl-l-homoserine lactone (C6HSL) hydrolytic QQ activity was detected in rhizosphere isolates namely Bacillus cereus G and Priestia aryabhattai J1D. The cell-free supernatant of the bacterial isolates indicated a reduction in biofilm formation in the human pathogens Vibrio cholerae, Pseudomonas aeruginosa, and Staphylococcus aureus without inhibiting cells, signifying their biocontrol property. Furthermore, liquid chromatography high resolution mass spectrometry analysis confirmed C6HSL hydrolytic activity by AHL lactonase produced by these rhizosphere isolates. Also, the aiiA homologous gene from the bacterial isolates showed similarity with the aiiA lactonase gene from Bacillus species, which was further confirmed by homology modelling. In silico structure analysis by comparing with the structure of Bacillus revealed the similarity in the active site, indicating the same degradation pattern. Based on available reported data, the present study indicates the first report of the presence of the aiiA lactonase gene in P. aryabhattai.
(© 2023. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)
Databáze: MEDLINE
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