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Appl. Environ. Microbiol., Dec 1996, 4410-4416, Vol 62, No. 12
Copyright © 1996, American Society for Microbiology

Purification and amino acid sequences of piscicocins V1a and V1b, two class IIa bacteriocins secreted by Carnobacterium piscicola V1 that display significantly different levels of specific inhibitory activity

P Bhugaloo-Vial, X Dousset, A Metivier, O Sorokine, P Anglade, P Boyaval and D Marion
Laboratoire de Microbiologie, Ecole Nationale d'Ingenieurs des Techniques des Industries Agricoles et Alimentaires, Nantes, France.

Two bacteriocins produced by Carnobacterium piscicola V1 were purified and characterized. Piscicocin V1a (molecular mass = 4,416 Da) and piscicocin V1b (molecular mass = 4,526 Da) are nonlantibiotic, small, heat-stable antibacterial peptides. Piscicocin V1b is identical to carnobacteriocin BM1, while piscicocin V1a is a new bacteriocin. Its complete sequence of 44 amino acid residues has been determined. Piscicocin V1a belongs to the class IIa bacteriocins having the consensus YGNGV motif. These peptides inhibit various gram-positive bacteria, including Listeria monocytogenes. Piscicocin V1a is approximately 100 times more active than piscicocin V1b against indicator strains. However, the antagonistic spectrum is the same for both piscicocins. Comparison of these results with the analysis of the amino acid sequence and secondary structure predictions suggests that (i) the conserved N-terminal conserved domain is involved in the receptor recognition and therefore in an "all-or-none" response against target bacterial cells and (ii) the C-terminal variable and hydrophobic domain determines membrane anchoring and therefore the intensity of the antagonist response.

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