TY - JOUR
T1 - Characterisation of the action mechanism of a Lactococcus-specific bacteriocin, lactococcin Z
AU - Daba, Ghoson Mosbah
AU - Ishibashi, Naoki
AU - Gong, Xiao
AU - Taki, Hiroya
AU - Yamashiro, Keisuke
AU - Lim, Yen Yi
AU - Zendo, Takeshi
AU - Sonomoto, Kenji
N1 - Funding Information:
This work was partially supported by JSPS KAKENHI grant numbers JP24380051 and JP17H0397 . We are grateful to the Ministry of Education, Culture, Sports, Science and Technology of Japan for providing a scholarship grant to G. M. Daba. No conflict of interest is declared.
Publisher Copyright:
© 2018 The Society for Biotechnology, Japan
PY - 2018/11
Y1 - 2018/11
N2 - 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.
AB - 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.
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U2 - 10.1016/j.jbiosc.2018.05.018
DO - 10.1016/j.jbiosc.2018.05.018
M3 - Article
C2 - 29929768
AN - SCOPUS:85048745858
SN - 1389-1723
VL - 126
SP - 603
EP - 610
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
IS - 5
ER -