LYSO

LYSO Mechanism of inhibition of Lactococcus piscium against Listeria monocytogenes

Functional characterization of the PG hydrolase (SCA91560.1) and of the LXG protein identified in L. piscium CNCM I-4031 in its inhibiting activity against Listeria monocytogenes

The PhD thesis of Taous Saraoui focused on the interaction mechanisms between a bio-protective bacterium Lactococcus piscium CNCM I-4031 and a pathogenic bacterium Listeria monocytogenes. This work showed that the mechanism of inhibition of L. piscium against L. monocytogenes did not involve the excretion of antimicrobial molecules or nutritional competition, but required contact between bacterial cells. The studies that followed within the framework of the COMBACT project aimed to identify the biochemical elements at the origin of this inhibition mechanism. A PG hydrolase (SCA91560.1) and LXG protein have been identified in L. piscium. The objective of LYSO is therefore to carry out a functional characterization of these two proteins. Several steps are envisaged to achieve this:

  •     The heterologous production of recombinant PG hydrolase in Escherichia coli followed by purification of the protein
  •     Evaluating the enzymatic activity of tthe recombinant PG hydrolase and its antimicrobial potential against targeted bacteria.
  •     The production of a mutant of L. piscium CNCM I-403 no longer producing the PG hydrolase and the LXG protein, and the consequences on its inhibitory capacities

Modification date : 11 September 2023 | Publication date : 18 December 2020 | Redactor : SG