Characterisation of the action mechanism of a Lactococcus-specific bacteriocin, lactococcin Z

Ghoson Mosbah Daba, Naoki Ishibashi, Xiao Gong, Hiroya Taki, Keisuke Yamashiro, Yen Yi Lim, Takeshi Zendo, Kenji Sonomoto

研究成果: ジャーナルへの寄稿記事

1 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)603-610
ページ数8
ジャーナルJournal of Bioscience and Bioengineering
126
発行部数5
DOI
出版物ステータス出版済み - 11 1 2018

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Lactococcus
Bacteriocins
Membranes
Carbon
Glucose
Genes
Lactococcus lactis
Mannose
lactococcin A
Galactose
Membrane Potentials
Immunity
Phosphotransferases
Cell Membrane

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

これを引用

Daba, G. M., Ishibashi, N., Gong, X., Taki, H., Yamashiro, K., Lim, Y. Y., ... Sonomoto, K. (2018). Characterisation of the action mechanism of a Lactococcus-specific bacteriocin, lactococcin Z. Journal of Bioscience and Bioengineering, 126(5), 603-610. https://doi.org/10.1016/j.jbiosc.2018.05.018

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, 巻 126, 番号 5, 01.11.2018, p. 603-610.

研究成果: ジャーナルへの寄稿記事

Daba, Ghoson Mosbah ; Ishibashi, Naoki ; Gong, Xiao ; Taki, Hiroya ; Yamashiro, Keisuke ; Lim, Yen Yi ; Zendo, Takeshi ; Sonomoto, Kenji. / Characterisation of the action mechanism of a Lactococcus-specific bacteriocin, lactococcin Z. :: Journal of Bioscience and Bioengineering. 2018 ; 巻 126, 番号 5. pp. 603-610.
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abstract = "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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