Compréhension des mécanismes physiologiques et génétiques impliqués dans l'activité réductrice de Lactococcus lactis

摘要

Lactic acid bacteria, particularly Lactococcus lactis are used in dairy industry. These bacteria are known to have a reducing activity, indicating their ability to lower the redox potential (Eh) of a medium. L. lactis MG1363 genome encodes several proteins with a CXXC motif, potentially linked with a redox activity. To understand the role of proteins rich in cysteine located at the surface of L. lactis, two approaches were used, one bioinformatics and biochemical another. For bioinformatic approach, interest was focused on two proteins of unknown function and CX2CX10CX2C motif: Llmg_0524 and Llmg_0526. Their corresponding genes form an operon temporarily induces in early growth phase. In these two proteins, the pattern chelate a zinc ion via its cysteine residues. The zinc-cysteine complexe is very stable, it suggests a probable role in protein stability. Data suggest that this operon contributes to the cell wall integrity. The identification of exofacial thiol proteins by a biochemical approach indicates that AhpF is present at the surface of L. lactis. The ahpF gene deletion causes a strong sensitivity to the cumene hydroperoxide, but no sensibility for hydrogen peroxide. In the mutant ahpF incubation with cumene hydroperoxide modified fatty acid proportion, cyclopropanation mechanism thus contributes to the survival in response to oxidative stress. Understanding the lactococci functions involved in the reduction activity allows a better control of redox potentiel in the fermented food production and thus a better control of foodbornes microorganisms in these products. Food-Redox project is financially supported by the French National Research Agency.