The commensal bacterium Lactobacillus plantarum has documented immunomodulatory properties, supporting its potential to serve a role in the regulation of inflammation within the human gut. The production of adhesins and, consequently, biofilm formation in L.plantarum is controlled by quorum sensing (QS). Despite the complete genome of species such as L.plantarum WCSF1 being sequenced, the native form of the peptide that controls QS, LamD, remains undefined given recent evidence of a pH-dependent intramolecular S-to-N acyl transfer. Our work seeks to define the active form through synthesis of the possible LamD variants and the construction of a β-glucuronidase reporter strain. Optimization of a β-glucurodinase QS assay has validated the design of the reporter strain, but has not yet revealed the identity of the peptide autoinducer.

Defining and modulating quorum sensing in Lactobacillus plantarum

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