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Characterisation of the action mechanism of a Lactococcus-specific bacteriocin, lactococcin Z
- Daba, Ghoson Mosbah, Ishibashi, Naoki, Gong, Xiao, Taki, Hiroya, Yamashiro, Keisuke, Lim, Yen Yi, Zendo, Takeshi, Sonomoto, Kenji
- Journal of bioscience and bioengineering 2018 v.126 no.5 pp. 603-610
- Lactococcus lactis, antibacterial properties, carbon, cross immunity, galactose, genes, glucose, lactococcins, mannose, membrane potential, mutants, mutation, receptors, transferases
- Lactococcin Z is a novel Lactococcus-specific bacteriocin produced by Lactococcus lactis QU 7 that shares 55.6% identity with lactococcin A. To identify the receptor targeted by lactococcin Z, several lactococcin Z-resistant mutants were generated from the sensitive strain, L. lactis IL1403. The resistant mutants showed difficulties in utilising mannose and glucose as sole carbon sources, contrary to their pattern of growth in the presence of galactose as a sole carbon source. Mutations were found in the ptnC and ptnD genes of lactococcin Z-resistant mutants, which encode the mannose phosphotransferase system (Man-PTS) components, IIC and IID, respectively; therefore, IIC and IID are proposed as potential receptors employed by lactococcin Z and are the same receptors targeted by lactococcin A. Both lactococcins A and Z share a high percentage identity in their N-termini regions in contrast to their C-termini that show less similarity; this may explain the difference in their action mechanisms as well as the lack of cross-immunity between them. Although lactococcin Z showed bactericidal activity, it neither dissipated membrane potential nor formed pores on the membranes of sensitive cells, in sharp contrast to the pore-forming lactococcin A.