The aim of this study was to show the differences that could exist at the physiological and structural levels between Enterococcus faecalis JH2-2 (wild type) and three mutant strains resistant to divercin RV41. These mutant strains were recently isolated and characterized for their intermediate resistance to recombinant DvnRV41; a subclass IIa bacteriocin produced by Escherichia coli. These mutant strains were named 35A1 (altered in gene coding phosphoesterase activity), 35H1 (altered in gene coding σ54 factor) and 36H4 (altered in gene coding glycerophosphodiesterase). The growth and resistance of each strain were tested against lysozyme. The inhibitory substance did not show any cross-resistance but exhibited an additive effect ascribed to the combined action of lysozyme and (P)-DvnRV41. The use of Fourier transform infrared spectroscopy (FT-IR) allowed to unravelling differences at the structural levels between the aforementioned strains. Thus, mutants 35H1 and 36H4 showed clear differences from mutant 35A1 and wild-type strain. These differences were located, mainly in the fatty acid region and in the polysaccharide composition. This study contributes to understanding more the resistance/sensitivity of Ent. faecalis to (P)-DvnRV41, a subclass IIa bacteriocin