TY  - JOUR
AU  - Uzelac, Gordana
AU  - Miljković, Marija
AU  - Lozo, Jelena
AU  - Radulović, Zorica
AU  - Tošić, Nataša
AU  - Kojić, Milan
PY  - 2015
UR  - http://intor.torlakinstitut.com/handle/123456789/741
AB  - The production of LsbB, leaderless class II bacteriocin, is encoded by genes (lsbB and lmrB) located on plasmid pMN5 in Lactococcus lactis BGMN1-5. Heterologous expression of the lsbB gene using the pAZIL vector (pAZIL-lsbB) in L. lactis subsp. cremoris MG7284 resulted in a significant reduction (more than 30 times) of bacteriocin LsbB expression. Subcloning and deletion experiments with plasmid pMN5 revealed that full expression of LsbB requires the presence of a complete transcription terminator located downstream of the lsbB gene. RNA stability analysis revealed that the presence of a transcription terminator increased the RNA stability by three times and the expression of LsbB by 30 times. The study of the influence of transcription terminator on the expression of other bacteriocin genes (lcnB, for lactococcin B production) indicated that this translational terminator likely functions in a lsbB-specific manner rather than in a general manner.
PB  - Elsevier Gmbh, Urban & Fischer Verlag, Jena
T2  - Microbiological Research
T1  - Expression of bacteriocin LsbB is dependent on a transcription terminator
EP  - 53
SP  - 45
VL  - 179
DO  - 10.1016/j.micres.2015.06.011
ER  - 

@article{
author = "Uzelac, Gordana and Miljković, Marija and Lozo, Jelena and Radulović, Zorica and Tošić, Nataša and Kojić, Milan",
year = "2015",
abstract = "The production of LsbB, leaderless class II bacteriocin, is encoded by genes (lsbB and lmrB) located on plasmid pMN5 in Lactococcus lactis BGMN1-5. Heterologous expression of the lsbB gene using the pAZIL vector (pAZIL-lsbB) in L. lactis subsp. cremoris MG7284 resulted in a significant reduction (more than 30 times) of bacteriocin LsbB expression. Subcloning and deletion experiments with plasmid pMN5 revealed that full expression of LsbB requires the presence of a complete transcription terminator located downstream of the lsbB gene. RNA stability analysis revealed that the presence of a transcription terminator increased the RNA stability by three times and the expression of LsbB by 30 times. The study of the influence of transcription terminator on the expression of other bacteriocin genes (lcnB, for lactococcin B production) indicated that this translational terminator likely functions in a lsbB-specific manner rather than in a general manner.",
publisher = "Elsevier Gmbh, Urban & Fischer Verlag, Jena",
journal = "Microbiological Research",
title = "Expression of bacteriocin LsbB is dependent on a transcription terminator",
pages = "53-45",
volume = "179",
doi = "10.1016/j.micres.2015.06.011"
}

Uzelac, G., Miljković, M., Lozo, J., Radulović, Z., Tošić, N.,& Kojić, M.. (2015). Expression of bacteriocin LsbB is dependent on a transcription terminator. in Microbiological Research
Elsevier Gmbh, Urban & Fischer Verlag, Jena., 179, 45-53.
https://doi.org/10.1016/j.micres.2015.06.011

Uzelac G, Miljković M, Lozo J, Radulović Z, Tošić N, Kojić M. Expression of bacteriocin LsbB is dependent on a transcription terminator. in Microbiological Research. 2015;179:45-53.
doi:10.1016/j.micres.2015.06.011 .

Uzelac, Gordana, Miljković, Marija, Lozo, Jelena, Radulović, Zorica, Tošić, Nataša, Kojić, Milan, "Expression of bacteriocin LsbB is dependent on a transcription terminator" in Microbiological Research, 179 (2015):45-53,
https://doi.org/10.1016/j.micres.2015.06.011 . .

TY  - JOUR
AU  - Ovchinnikov, Kirill V.
AU  - Kristiansen, Per E.
AU  - Uzelac, Gordana
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
AU  - Nissen-Meyer, Jon
AU  - Nes, Ingolf F.
AU  - Diep, Dzung B.
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/750
UR  - http://intor.torlakinstitut.com/handle/123456789/728
AB  - Background: The bacteriocin LsbB targets a membrane-bound zinc-dependent peptidase. Results: The structure of LsbB was resolved by NMR. The C-terminal unstructured domains of LsbB and several other related bacteriocins were responsible for receptor binding. Conclusion: A subgroup of leaderless bacteriocins has been found to share a similar mechanism in receptor recognition. Significance: The study highlights the structure-function relationship of LsbB. LsbB is a class II leaderless lactococcal bacteriocin of 30 amino acids. In the present work, the structure and function relationship of LsbB was assessed. Structure determination by NMR spectroscopy showed that LsbB has an N-terminal -helix, whereas the C-terminal of the molecule remains unstructured. To define the receptor binding domain of LsbB, a competition assay was performed in which a systematic collection of truncated peptides of various lengths covering different parts of LsbB was used to inhibit the antimicrobial activity of LsbB. The results indicate that the outmost eight-amino acid sequence at the C-terminal end is likely to contain the receptor binding domain because only truncated fragments from this region could antagonize the antimicrobial activity of LsbB. Furthermore, alanine substitution revealed that the tryptophan in position 25 (Trp(25)) is crucial for the blocking activity of the truncated peptides, as well as for the antimicrobial activity of the full-length bacteriocin. LsbB shares significant sequence homology with five other leaderless bacteriocins, especially at their C-terminal halves where all contain a conserved KXXXGXXPWE motif, suggesting that they might recognize the same receptor as LsbB. This notion was supported by the fact that truncated peptides with sequences derived from the C-terminal regions of two LsbB-related bacteriocins inhibited the activity of LsbB, in the same manner as found with the truncated version of LsbB. Taken together, these structure-function studies provide strong evidence that the receptor-binding parts of LsbB and sequence-related bacteriocins are located in their C-terminal halves.
PB  - Amer Soc Biochemistry Molecular Biology Inc, Bethesda
T2  - Journal of Biological Chemistry
T1  - Defining the Structure and Receptor Binding Domain of the Leaderless Bacteriocin LsbB
EP  - 23845
IS  - 34
SP  - 23838
VL  - 289
DO  - 10.1074/jbc.M114.579698
ER  - 

@article{
author = "Ovchinnikov, Kirill V. and Kristiansen, Per E. and Uzelac, Gordana and Topisirović, Ljubiša and Kojić, Milan and Nissen-Meyer, Jon and Nes, Ingolf F. and Diep, Dzung B.",
year = "2014",
abstract = "Background: The bacteriocin LsbB targets a membrane-bound zinc-dependent peptidase. Results: The structure of LsbB was resolved by NMR. The C-terminal unstructured domains of LsbB and several other related bacteriocins were responsible for receptor binding. Conclusion: A subgroup of leaderless bacteriocins has been found to share a similar mechanism in receptor recognition. Significance: The study highlights the structure-function relationship of LsbB. LsbB is a class II leaderless lactococcal bacteriocin of 30 amino acids. In the present work, the structure and function relationship of LsbB was assessed. Structure determination by NMR spectroscopy showed that LsbB has an N-terminal -helix, whereas the C-terminal of the molecule remains unstructured. To define the receptor binding domain of LsbB, a competition assay was performed in which a systematic collection of truncated peptides of various lengths covering different parts of LsbB was used to inhibit the antimicrobial activity of LsbB. The results indicate that the outmost eight-amino acid sequence at the C-terminal end is likely to contain the receptor binding domain because only truncated fragments from this region could antagonize the antimicrobial activity of LsbB. Furthermore, alanine substitution revealed that the tryptophan in position 25 (Trp(25)) is crucial for the blocking activity of the truncated peptides, as well as for the antimicrobial activity of the full-length bacteriocin. LsbB shares significant sequence homology with five other leaderless bacteriocins, especially at their C-terminal halves where all contain a conserved KXXXGXXPWE motif, suggesting that they might recognize the same receptor as LsbB. This notion was supported by the fact that truncated peptides with sequences derived from the C-terminal regions of two LsbB-related bacteriocins inhibited the activity of LsbB, in the same manner as found with the truncated version of LsbB. Taken together, these structure-function studies provide strong evidence that the receptor-binding parts of LsbB and sequence-related bacteriocins are located in their C-terminal halves.",
publisher = "Amer Soc Biochemistry Molecular Biology Inc, Bethesda",
journal = "Journal of Biological Chemistry",
title = "Defining the Structure and Receptor Binding Domain of the Leaderless Bacteriocin LsbB",
pages = "23845-23838",
number = "34",
volume = "289",
doi = "10.1074/jbc.M114.579698"
}

Ovchinnikov, K. V., Kristiansen, P. E., Uzelac, G., Topisirović, L., Kojić, M., Nissen-Meyer, J., Nes, I. F.,& Diep, D. B.. (2014). Defining the Structure and Receptor Binding Domain of the Leaderless Bacteriocin LsbB. in Journal of Biological Chemistry
Amer Soc Biochemistry Molecular Biology Inc, Bethesda., 289(34), 23838-23845.
https://doi.org/10.1074/jbc.M114.579698

Ovchinnikov KV, Kristiansen PE, Uzelac G, Topisirović L, Kojić M, Nissen-Meyer J, Nes IF, Diep DB. Defining the Structure and Receptor Binding Domain of the Leaderless Bacteriocin LsbB. in Journal of Biological Chemistry. 2014;289(34):23838-23845.
doi:10.1074/jbc.M114.579698 .

Ovchinnikov, Kirill V., Kristiansen, Per E., Uzelac, Gordana, Topisirović, Ljubiša, Kojić, Milan, Nissen-Meyer, Jon, Nes, Ingolf F., Diep, Dzung B., "Defining the Structure and Receptor Binding Domain of the Leaderless Bacteriocin LsbB" in Journal of Biological Chemistry, 289, no. 34 (2014):23838-23845,
https://doi.org/10.1074/jbc.M114.579698 . .

TY  - JOUR
AU  - Terzić-Vidojević, Amarela
AU  - Mihajlović, Sanja
AU  - Uzelac, Gordana
AU  - Golić, Nataša
AU  - Fira, Đorđe
AU  - Kojić, Milan
AU  - Topisirović, Ljubiša
PY  - 2014
UR  - http://intor.torlakinstitut.com/handle/123456789/751
AB  - The aim of this study was to identify and characterize the lactic acid bacteria (LAB) of artisanal Golija raw and cooked cows' milk cheeses traditionally manufactured without the addition of starter culture. A total of 188 Gram-positive and catalase-negative isolates of Golija cheeses were obtained from seven samples of different ripening time. Phenotype-based assays as well as rep-PCR and 16S rDNA sequence analysis were undertaken for all 188 LAB strains. The most diverse species were isolated from 20-day-old BGGO8 cheese (Lactobacillus fermentum, Lactobacillus plantarum, Lactobacillus casei/paracasei, Lactobacillus sucicola, Lactococcus lactis subsp. lactis, Lactococcus lactis subsp. lactis by. diacetylactis, Enterococcus faecium, Enterococcus durans and Leuconostoc mesenteroides). In other Golija cheeses Lactobacillus reuteri, Lactobacillus curvatus, Lactobacillus rhamnosus, Lactococcus lactis subsp. cremoris, Lactococcus garvieae, Streptococcus thermophilus and Leuconostoc pseudomesenteroides were found. Pronounced antimicrobial properties showed enterococci (13/42) and lactococci (12/31), while the good proteolytic activity demonstrated lactococci (13/31) and lactobacilli (10/29).
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Identification and characterization of lactic acid bacteria isolated from artisanal white brined Golija cows' milk cheeses
EP  - 192
IS  - 1
SP  - 179
VL  - 66
DO  - 10.2298/ABS1401179T
ER  - 

@article{
author = "Terzić-Vidojević, Amarela and Mihajlović, Sanja and Uzelac, Gordana and Golić, Nataša and Fira, Đorđe and Kojić, Milan and Topisirović, Ljubiša",
year = "2014",
abstract = "The aim of this study was to identify and characterize the lactic acid bacteria (LAB) of artisanal Golija raw and cooked cows' milk cheeses traditionally manufactured without the addition of starter culture. A total of 188 Gram-positive and catalase-negative isolates of Golija cheeses were obtained from seven samples of different ripening time. Phenotype-based assays as well as rep-PCR and 16S rDNA sequence analysis were undertaken for all 188 LAB strains. The most diverse species were isolated from 20-day-old BGGO8 cheese (Lactobacillus fermentum, Lactobacillus plantarum, Lactobacillus casei/paracasei, Lactobacillus sucicola, Lactococcus lactis subsp. lactis, Lactococcus lactis subsp. lactis by. diacetylactis, Enterococcus faecium, Enterococcus durans and Leuconostoc mesenteroides). In other Golija cheeses Lactobacillus reuteri, Lactobacillus curvatus, Lactobacillus rhamnosus, Lactococcus lactis subsp. cremoris, Lactococcus garvieae, Streptococcus thermophilus and Leuconostoc pseudomesenteroides were found. Pronounced antimicrobial properties showed enterococci (13/42) and lactococci (12/31), while the good proteolytic activity demonstrated lactococci (13/31) and lactobacilli (10/29).",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Identification and characterization of lactic acid bacteria isolated from artisanal white brined Golija cows' milk cheeses",
pages = "192-179",
number = "1",
volume = "66",
doi = "10.2298/ABS1401179T"
}

Terzić-Vidojević, A., Mihajlović, S., Uzelac, G., Golić, N., Fira, Đ., Kojić, M.,& Topisirović, L.. (2014). Identification and characterization of lactic acid bacteria isolated from artisanal white brined Golija cows' milk cheeses. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 66(1), 179-192.
https://doi.org/10.2298/ABS1401179T

Terzić-Vidojević A, Mihajlović S, Uzelac G, Golić N, Fira Đ, Kojić M, Topisirović L. Identification and characterization of lactic acid bacteria isolated from artisanal white brined Golija cows' milk cheeses. in Archives of Biological Sciences. 2014;66(1):179-192.
doi:10.2298/ABS1401179T .

Terzić-Vidojević, Amarela, Mihajlović, Sanja, Uzelac, Gordana, Golić, Nataša, Fira, Đorđe, Kojić, Milan, Topisirović, Ljubiša, "Identification and characterization of lactic acid bacteria isolated from artisanal white brined Golija cows' milk cheeses" in Archives of Biological Sciences, 66, no. 1 (2014):179-192,
https://doi.org/10.2298/ABS1401179T . .

TY  - JOUR
AU  - Terzić-Vidojević, Amarela
AU  - Mihajlović, Sanja
AU  - Uzelac, Gordana
AU  - Veljović, Katarina
AU  - Tolinački, Maja
AU  - Živković, Milica
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2014
UR  - http://intor.torlakinstitut.com/handle/123456789/716
AB  - The aim of this study was to investigate the composition of lactic acid bacteria (LAB) in autochthonous young cheeses, sweet creams and sweet kajmaks produced in the Vlasic mountain region of central Bosnia and Herzegovina near the town of Travnik over a four season period. These three products were made from cow's milk by a traditional method without the addition of a starter culture. Preliminary characterization with phenotype-based assays and identification using rep-PCR with a (GTG)(5) primer and 16S rDNA sequence analysis were undertaken for 460 LAB isolates obtained from all the examined samples. Fifteen species were identified as follows: Lactococcus lactis, Lactococcus raffinolactis, Lactococcus garviae, Lactobacillus casei, Lactobacillus plantarum, Lactobacillus helveticus, Enterococcus faecium, Enterococcus durans, Enterococcus faecalis, Enterococcus italicus, Leuconostoc mesenteroides, Leuconostoc pseudomesenteroides, Leuconostoc lactis, Streptococcus thermophilus and Streptococcus mitis. A wide genotypic and phenotypic heterogeneity of the species was observed, particularly within the Lc. lactis strains. In all of the tested dairy products across four seasons, a significantly positive correlation (r = 0.690) between the presence of lactococci and enterococci and a negative correlation (r = 0.722) between the presence of lactococci and leuconostocs were recorded. Forty-five percent of the lactobacilli and 54.4% of the lactococci exhibited proteolytic activity, whereas 18.7% of the total LAB isolates exhibited antimicrobial activity.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Food Microbiology
T1  - Characterization of lactic acid bacteria isolated from artisanal Travnik young cheeses, sweet creams and sweet kajmaks over four seasons
EP  - 38
SP  - 27
VL  - 39
DO  - 10.1016/j.fm.2013.10.011
ER  - 

@article{
author = "Terzić-Vidojević, Amarela and Mihajlović, Sanja and Uzelac, Gordana and Veljović, Katarina and Tolinački, Maja and Živković, Milica and Topisirović, Ljubiša and Kojić, Milan",
year = "2014",
abstract = "The aim of this study was to investigate the composition of lactic acid bacteria (LAB) in autochthonous young cheeses, sweet creams and sweet kajmaks produced in the Vlasic mountain region of central Bosnia and Herzegovina near the town of Travnik over a four season period. These three products were made from cow's milk by a traditional method without the addition of a starter culture. Preliminary characterization with phenotype-based assays and identification using rep-PCR with a (GTG)(5) primer and 16S rDNA sequence analysis were undertaken for 460 LAB isolates obtained from all the examined samples. Fifteen species were identified as follows: Lactococcus lactis, Lactococcus raffinolactis, Lactococcus garviae, Lactobacillus casei, Lactobacillus plantarum, Lactobacillus helveticus, Enterococcus faecium, Enterococcus durans, Enterococcus faecalis, Enterococcus italicus, Leuconostoc mesenteroides, Leuconostoc pseudomesenteroides, Leuconostoc lactis, Streptococcus thermophilus and Streptococcus mitis. A wide genotypic and phenotypic heterogeneity of the species was observed, particularly within the Lc. lactis strains. In all of the tested dairy products across four seasons, a significantly positive correlation (r = 0.690) between the presence of lactococci and enterococci and a negative correlation (r = 0.722) between the presence of lactococci and leuconostocs were recorded. Forty-five percent of the lactobacilli and 54.4% of the lactococci exhibited proteolytic activity, whereas 18.7% of the total LAB isolates exhibited antimicrobial activity.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Food Microbiology",
title = "Characterization of lactic acid bacteria isolated from artisanal Travnik young cheeses, sweet creams and sweet kajmaks over four seasons",
pages = "38-27",
volume = "39",
doi = "10.1016/j.fm.2013.10.011"
}

Terzić-Vidojević, A., Mihajlović, S., Uzelac, G., Veljović, K., Tolinački, M., Živković, M., Topisirović, L.,& Kojić, M.. (2014). Characterization of lactic acid bacteria isolated from artisanal Travnik young cheeses, sweet creams and sweet kajmaks over four seasons. in Food Microbiology
Academic Press Ltd- Elsevier Science Ltd, London., 39, 27-38.
https://doi.org/10.1016/j.fm.2013.10.011

Terzić-Vidojević A, Mihajlović S, Uzelac G, Veljović K, Tolinački M, Živković M, Topisirović L, Kojić M. Characterization of lactic acid bacteria isolated from artisanal Travnik young cheeses, sweet creams and sweet kajmaks over four seasons. in Food Microbiology. 2014;39:27-38.
doi:10.1016/j.fm.2013.10.011 .

Terzić-Vidojević, Amarela, Mihajlović, Sanja, Uzelac, Gordana, Veljović, Katarina, Tolinački, Maja, Živković, Milica, Topisirović, Ljubiša, Kojić, Milan, "Characterization of lactic acid bacteria isolated from artisanal Travnik young cheeses, sweet creams and sweet kajmaks over four seasons" in Food Microbiology, 39 (2014):27-38,
https://doi.org/10.1016/j.fm.2013.10.011 . .

TY  - 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 . .