Biodiversity of N-acyl homoserine lactonase (aiiA) gene from Bacillus subtilis

Document Type

Article

Publication Date

2022

Abstract

Microorganisms rely on the benefit of using chemical signals called autoinducers (AIs) as a connection matter in term of population, this mechanism is known as quorum sensing (QS). Quorum sensing is responsible for formation of biofilm together with virulence in bacteria. The most known QS molecule is N-acyl homoserine lactones (AHLs). A lot of degrading enzymes including lactonases that open the AHL ring and acylases that breakdown its acyl side chain can degrade or inactivate AHL. Due to similarity in lactone ring structure among AHLs it is susceptible to most of lactonases. Bacillus species are among the most promising bacteria producing AHL-lactonase. The aim of the work is to identify and study the diversity of the AHL-Lactonase gene among different Bacillus subtilis as a promising Quorum Quenching (QQ) strategy to prevent bacterial infections and biofilm formation. The AHL-lactonase (aiiA) gene of 64 B. subtilis isolates was amplified and sequenced followed by multiple sequence alignment of the translated amino acid sequences, homology modeling and docking study. An expected PCR product of about 750 base pair was detected in 22 B. subtilis isolates, and the results revealed that the isolates’ sequences showed identity ranged between 97.61% and 99.47% with those in the NCBI GenBank database with 100% query coverage and 0.0 E-value. In addition, the results revealed high level of identity between many aiiA gene sequences of our isolates as they were closely related to the same sequences to many sequences of the NCBI GenBank database. The alignment of the amino acid sequences from the 22 B. subtilis isolates indicated that 84.4% of the amino acid residues were conserved between the aligned sequences. Docking of the co-crystalized ligand to wildtype and H109Y mutated protein showed a significant reduction of docking score for the mutated protein. This result indicate that this mutation might affect recognition or at least kinetics of these enzymes and hence their roles in quorum-quenching.

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