A Zn-Dependent Metallopeptidase Is Responsible for Sensitivity to LsbB, a Class II Leaderless Bacteriocin of Lactococcus lactis subsp lactis BGMN1-5
Аутори
Uzelac, GordanaKojić, Milan
Lozo, Jelena
Aleksandrzak-Piekarczyk, Tamara
Gabrielsen, Christina
Kristensen, Tom
Nes, Ingolf F.
Diep, Dzung B.
Topisirović, Ljubiša
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Lactococcus lactis subsp. lactis BGMN1-5 produces a leaderless class II bacteriocin called LsbB. To identify the receptor for LsbB, a cosmid library of the LsbB-sensitive strain BGMN1-596 was constructed. About 150 cosmid clones were individually isolated and transferred to LsbB-resistant mutants of BGMN1-596. Cosmid pAZILcos/MN2, carrying a 40-kb insert, was found to restore LsbB sensitivity in LsbB-resistant mutants. Further subcloning revealed that a 1.9-kb fragment, containing only one open reading frame, was sufficient to restore sensitivity. The fragment contains the gene yvjB coding for a Zn-dependent membrane-bound metallopeptidase, suggesting that this gene may serve as the receptor for LsbB. Further support for this notion derives from several independent experiments: (i) whole-genome sequencing confirmed that all LsbB-resistant mutants contain mutations in yvjB; (ii) disruption of yvjB by direct gene knockout rendered sensitive strains BGMN1-596 and IL1403 resistant to LsbB;... and (iii) most compellingly, heterologous expression of yvjB in naturally resistant strains of other species, such as Lactobacillus paracasei and Enterococcus faecalis, also rendered them sensitive to the bacteriocin. To our knowledge, this is the first time a membrane-bound peptidase gene has been shown to be involved in bacteriocin sensitivity in target cells. We also demonstrated a novel successful approach for identifying bacteriocin receptors.
Извор:
Journal of Bacteriology, 2013, 195, 24, 5614-5621Издавач:
- Amer Soc Microbiology, Washington
Финансирање / пројекти:
- Изучавање гена и молекуларних механизама у основи пробиотичке активности бактерија млечне киселине изолованих са подручја западног Балкана (RS-MESTD-Basic Research (BR or ON)-173019)
- NOCC
DOI: 10.1128/JB.00859-13
ISSN: 0021-9193
PubMed: 24123824
WoS: 000327546900020
Scopus: 2-s2.0-84890251217
URI
https://imagine.imgge.bg.ac.rs/handle/123456789/703http://intor.torlakinstitut.com/handle/123456789/683
Институција/група
TorlakTY - JOUR AU - Uzelac, Gordana AU - Kojić, Milan AU - Lozo, Jelena AU - Aleksandrzak-Piekarczyk, Tamara AU - Gabrielsen, Christina AU - Kristensen, Tom AU - Nes, Ingolf F. AU - Diep, Dzung B. AU - Topisirović, Ljubiša PY - 2013 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/703 UR - http://intor.torlakinstitut.com/handle/123456789/683 AB - Lactococcus lactis subsp. lactis BGMN1-5 produces a leaderless class II bacteriocin called LsbB. To identify the receptor for LsbB, a cosmid library of the LsbB-sensitive strain BGMN1-596 was constructed. About 150 cosmid clones were individually isolated and transferred to LsbB-resistant mutants of BGMN1-596. Cosmid pAZILcos/MN2, carrying a 40-kb insert, was found to restore LsbB sensitivity in LsbB-resistant mutants. Further subcloning revealed that a 1.9-kb fragment, containing only one open reading frame, was sufficient to restore sensitivity. The fragment contains the gene yvjB coding for a Zn-dependent membrane-bound metallopeptidase, suggesting that this gene may serve as the receptor for LsbB. Further support for this notion derives from several independent experiments: (i) whole-genome sequencing confirmed that all LsbB-resistant mutants contain mutations in yvjB; (ii) disruption of yvjB by direct gene knockout rendered sensitive strains BGMN1-596 and IL1403 resistant to LsbB; and (iii) most compellingly, heterologous expression of yvjB in naturally resistant strains of other species, such as Lactobacillus paracasei and Enterococcus faecalis, also rendered them sensitive to the bacteriocin. To our knowledge, this is the first time a membrane-bound peptidase gene has been shown to be involved in bacteriocin sensitivity in target cells. We also demonstrated a novel successful approach for identifying bacteriocin receptors. PB - Amer Soc Microbiology, Washington T2 - Journal of Bacteriology T1 - A Zn-Dependent Metallopeptidase Is Responsible for Sensitivity to LsbB, a Class II Leaderless Bacteriocin of Lactococcus lactis subsp lactis BGMN1-5 EP - 5621 IS - 24 SP - 5614 VL - 195 DO - 10.1128/JB.00859-13 ER -
@article{ author = "Uzelac, Gordana and Kojić, Milan and Lozo, Jelena and Aleksandrzak-Piekarczyk, Tamara and Gabrielsen, Christina and Kristensen, Tom and Nes, Ingolf F. and Diep, Dzung B. and Topisirović, Ljubiša", year = "2013", abstract = "Lactococcus lactis subsp. lactis BGMN1-5 produces a leaderless class II bacteriocin called LsbB. To identify the receptor for LsbB, a cosmid library of the LsbB-sensitive strain BGMN1-596 was constructed. About 150 cosmid clones were individually isolated and transferred to LsbB-resistant mutants of BGMN1-596. Cosmid pAZILcos/MN2, carrying a 40-kb insert, was found to restore LsbB sensitivity in LsbB-resistant mutants. Further subcloning revealed that a 1.9-kb fragment, containing only one open reading frame, was sufficient to restore sensitivity. The fragment contains the gene yvjB coding for a Zn-dependent membrane-bound metallopeptidase, suggesting that this gene may serve as the receptor for LsbB. Further support for this notion derives from several independent experiments: (i) whole-genome sequencing confirmed that all LsbB-resistant mutants contain mutations in yvjB; (ii) disruption of yvjB by direct gene knockout rendered sensitive strains BGMN1-596 and IL1403 resistant to LsbB; and (iii) most compellingly, heterologous expression of yvjB in naturally resistant strains of other species, such as Lactobacillus paracasei and Enterococcus faecalis, also rendered them sensitive to the bacteriocin. To our knowledge, this is the first time a membrane-bound peptidase gene has been shown to be involved in bacteriocin sensitivity in target cells. We also demonstrated a novel successful approach for identifying bacteriocin receptors.", publisher = "Amer Soc Microbiology, Washington", journal = "Journal of Bacteriology", title = "A Zn-Dependent Metallopeptidase Is Responsible for Sensitivity to LsbB, a Class II Leaderless Bacteriocin of Lactococcus lactis subsp lactis BGMN1-5", pages = "5621-5614", number = "24", volume = "195", doi = "10.1128/JB.00859-13" }
Uzelac, G., Kojić, M., Lozo, J., Aleksandrzak-Piekarczyk, T., Gabrielsen, C., Kristensen, T., Nes, I. F., Diep, D. B.,& Topisirović, L.. (2013). A Zn-Dependent Metallopeptidase Is Responsible for Sensitivity to LsbB, a Class II Leaderless Bacteriocin of Lactococcus lactis subsp lactis BGMN1-5. in Journal of Bacteriology Amer Soc Microbiology, Washington., 195(24), 5614-5621. https://doi.org/10.1128/JB.00859-13
Uzelac G, Kojić M, Lozo J, Aleksandrzak-Piekarczyk T, Gabrielsen C, Kristensen T, Nes IF, Diep DB, Topisirović L. A Zn-Dependent Metallopeptidase Is Responsible for Sensitivity to LsbB, a Class II Leaderless Bacteriocin of Lactococcus lactis subsp lactis BGMN1-5. in Journal of Bacteriology. 2013;195(24):5614-5621. doi:10.1128/JB.00859-13 .
Uzelac, Gordana, Kojić, Milan, Lozo, Jelena, Aleksandrzak-Piekarczyk, Tamara, Gabrielsen, Christina, Kristensen, Tom, Nes, Ingolf F., Diep, Dzung B., Topisirović, Ljubiša, "A Zn-Dependent Metallopeptidase Is Responsible for Sensitivity to LsbB, a Class II Leaderless Bacteriocin of Lactococcus lactis subsp lactis BGMN1-5" in Journal of Bacteriology, 195, no. 24 (2013):5614-5621, https://doi.org/10.1128/JB.00859-13 . .