title: Possible Correlation Between Bile Salt Hydrolysis and AHL Deamidation: Staphylococcus epidermidis RM1, a Potent Quorum Quencher and Bile Salt Hydrolase Producer.
abstract: The aim of the present work was to isolate a bile salt hydrolase (BSH) producer from fermented soy curd and explore the ability of the BSH produced to cleave bacterial quorum sensing signals. Bacterial isolates with possible ability to deconjugate bile salts were enriched and isolated on De Man, Rogosa and Sharpe (MRS) medium containing 0.2% bile salts. BSH-producing positive isolate with orange-pink-pigmented colonies was isolated and was identified as a strain of Staphylococcus epidermidis using biochemical and phylogenetic tools. S. epidermidis RM1 was shown to possess both potent BSH and N-acyl homoserine lactone (AHL) cleavage activity. Genetic basis of this dual-enzyme activity was explored by means of specific primers designed using S. epidermidis ATCC 12228 genome as template. It was observed that a single enzyme was not responsible for both the activity. Two different genetic elements corresponding to each of the enzymatic activity were successfully amplified from the genomic DNA of the isolate.
authors: Division of Biochemical Sciences, National Chemical Laboratory, Pune, 411008, India.
authors: Ruchira
authors: R
authors: Mukherji
authors: Asmita
authors: A
authors: Prabhune
mesh_terms: D054742:Acyl-Butyrolactones / Q000737:chemistry / Q000378:metabolism; D000581:Amidohydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001647:Bile Acids and Salts / Q000737:chemistry / Q000378:metabolism; D053038:Quorum Sensing / Q000502:physiology*; D013291:Streptococcus / Q000201:enzymology / Q000235:genetics
chemical_list: D054742:Acyl-Butyrolactones; D001426:Bacterial Proteins; D001647:Bile Acids and Salts; D000581:Amidohydrolases; C023154:choloylglycine hydrolase