In vivo activities of recombinant divercin V41 and its structural variants against Listeria monocytogenes.

Recombinant divercin RV41 (DvnRV41) and its structural variants were used in this study to assess their antilisterial activities in vivo in mice challenged intravenously with Listeria monocytogenes EGDe. Treatment with DvnRV41 before and after infection permitted a conclusion as to the capacities of this peptide to retain activity and reduce growth of L. monocytogenes EGDe.

Insights into structure-activity relationships in the C-terminal region of divercin V41, a class IIa bacteriocin with high-level antilisterial activity.

Divercin V41 (DvnV41) is a class IIa bacteriocin with potent antilisterial activity isolated from Carnobacterium divergens V41. Previously, we expressed from a synthetic gene, in Escherichia coli Origami, a recombinant DvnV41 designated DvnRV41, which possesses four additional amino acids (AMDP) in the N-terminal region that result from enzymatic cleavage and retains the initial DvnV41 activity. To unravel the relationship between the structure of DvnRV41 and its particularly elevated activity, we produced by site-directed mutagenesis eight variants in which a single amino acid replacement was specifically introduced into the sequence.

Antimicrobial activity of divercin RV41 produced and secreted by Lactococcus lactis.

Divercin V41 is a class IIa bacteriocin produced by Carnobacterium divergens V41 with a strong anti-Listeria activity. We have previously produced a recombinant form of divercin V41 (DvnRV41) in Escherichia coli strain Origami, by cloning a synthetic gene that codes for a mature divercin RV41 peptide. In this work we describe the inducible expression and secretion of DvnRV41 in the food-grade lactic acid bacterium, Lactococcus lactis.