TY  - JOUR
AU  - Mirković, Nemanja
AU  - Kulas, Jelena
AU  - Miloradović, Zorana
AU  - Miljković, Marija
AU  - Tucović, Dina
AU  - Miočinović, Jelena
AU  - Jovcić, Branko
AU  - Mirkov, Ivana
AU  - Kojić, Milan
PY  - 2020
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/5345
AB  - In last two decades, there has been a strong trend in the application of lactic acid bacteria as adjunctive cultures to control growth of spoilage and pathogenic bacteria in food. One of the most important properties that contribute to the application of these bacteria is the production of antimicrobial molecules. Lactococcus lactis subsp. lactis BGBU1-4, isolated from traditional brined cheese, produces thermostable bacteriocin named lactolisterin BU, with broad spectrum of activity against spoilage bacteria and foodborne pathogens. In this study, effect of strain BGBU1-4, as adjunct culture, on the numbers of Listeria monocytogenes ATCC19111 and Staphylococcus aureus LMM322 in artificially contaminated Quark-type, soft acid coagulated cheese, was examined. In addition, we analyzed influence of BGBU1-4 on chemical and sensory properties of the cheese, as well as immunological response of Albino oxford rats fed with Quark-type of cheese made using BGBU1-4 as adjunct culture. Results of this study revealed antibacterial potential of strain BGBU1-4 against L. monocytogenes ATCC19111 and S. aureus LMM322 in Quark-type cheese during 21 days of storage at 4 degrees C. Also, it was noticed the ability of BGBU1-4 to control the spontaneously grown yeasts and molds. Chemical composition and pH values of cheese containing BGBU1-4 were unchanged in comparison to control. The sensory quality scores showed that there was difference between cheese with and without adjunct culture in terms of flavor and oral texture, while for the odor and appearance no differences between two cheese variants were scored. Results of the immunological response of Albino rats fed with Quark-type cheese containing BGBU1-4 indicate absence of systematic inflammation. However, increased pro-inflammatory cytokines content (IL-1 beta, IL-6, IL-17) in intestine of rats fed with cheese containing BGBU1-4, concomitantly with unchanged anti-inflammatory cytokines suggests disruption of gut homeostasis and inflammation in this tissue. The changes caused by BGBU1-4 are reversible, system returns into homeostasis seven days after cessation of feeding with cheese containing BGBU1-4.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Control
T1  - Lactolisterin BU-producer Lactococcus lactis subsp. lactis BGBU1-4: Biocontrol of Listeria monocytogenes and Staphylocococcus aureus in fresh soft cheese and effect on immunological response of rats
VL  - 111
DO  - 10.1016/j.foodcont.2019.107076
ER  - 

@article{
author = "Mirković, Nemanja and Kulas, Jelena and Miloradović, Zorana and Miljković, Marija and Tucović, Dina and Miočinović, Jelena and Jovcić, Branko and Mirkov, Ivana and Kojić, Milan",
year = "2020",
abstract = "In last two decades, there has been a strong trend in the application of lactic acid bacteria as adjunctive cultures to control growth of spoilage and pathogenic bacteria in food. One of the most important properties that contribute to the application of these bacteria is the production of antimicrobial molecules. Lactococcus lactis subsp. lactis BGBU1-4, isolated from traditional brined cheese, produces thermostable bacteriocin named lactolisterin BU, with broad spectrum of activity against spoilage bacteria and foodborne pathogens. In this study, effect of strain BGBU1-4, as adjunct culture, on the numbers of Listeria monocytogenes ATCC19111 and Staphylococcus aureus LMM322 in artificially contaminated Quark-type, soft acid coagulated cheese, was examined. In addition, we analyzed influence of BGBU1-4 on chemical and sensory properties of the cheese, as well as immunological response of Albino oxford rats fed with Quark-type of cheese made using BGBU1-4 as adjunct culture. Results of this study revealed antibacterial potential of strain BGBU1-4 against L. monocytogenes ATCC19111 and S. aureus LMM322 in Quark-type cheese during 21 days of storage at 4 degrees C. Also, it was noticed the ability of BGBU1-4 to control the spontaneously grown yeasts and molds. Chemical composition and pH values of cheese containing BGBU1-4 were unchanged in comparison to control. The sensory quality scores showed that there was difference between cheese with and without adjunct culture in terms of flavor and oral texture, while for the odor and appearance no differences between two cheese variants were scored. Results of the immunological response of Albino rats fed with Quark-type cheese containing BGBU1-4 indicate absence of systematic inflammation. However, increased pro-inflammatory cytokines content (IL-1 beta, IL-6, IL-17) in intestine of rats fed with cheese containing BGBU1-4, concomitantly with unchanged anti-inflammatory cytokines suggests disruption of gut homeostasis and inflammation in this tissue. The changes caused by BGBU1-4 are reversible, system returns into homeostasis seven days after cessation of feeding with cheese containing BGBU1-4.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Control",
title = "Lactolisterin BU-producer Lactococcus lactis subsp. lactis BGBU1-4: Biocontrol of Listeria monocytogenes and Staphylocococcus aureus in fresh soft cheese and effect on immunological response of rats",
volume = "111",
doi = "10.1016/j.foodcont.2019.107076"
}

Mirković, N., Kulas, J., Miloradović, Z., Miljković, M., Tucović, D., Miočinović, J., Jovcić, B., Mirkov, I.,& Kojić, M.. (2020). Lactolisterin BU-producer Lactococcus lactis subsp. lactis BGBU1-4: Biocontrol of Listeria monocytogenes and Staphylocococcus aureus in fresh soft cheese and effect on immunological response of rats. in Food Control
Elsevier Sci Ltd, Oxford., 111.
https://doi.org/10.1016/j.foodcont.2019.107076

Mirković N, Kulas J, Miloradović Z, Miljković M, Tucović D, Miočinović J, Jovcić B, Mirkov I, Kojić M. Lactolisterin BU-producer Lactococcus lactis subsp. lactis BGBU1-4: Biocontrol of Listeria monocytogenes and Staphylocococcus aureus in fresh soft cheese and effect on immunological response of rats. in Food Control. 2020;111.
doi:10.1016/j.foodcont.2019.107076 .

Mirković, Nemanja, Kulas, Jelena, Miloradović, Zorana, Miljković, Marija, Tucović, Dina, Miočinović, Jelena, Jovcić, Branko, Mirkov, Ivana, Kojić, Milan, "Lactolisterin BU-producer Lactococcus lactis subsp. lactis BGBU1-4: Biocontrol of Listeria monocytogenes and Staphylocococcus aureus in fresh soft cheese and effect on immunological response of rats" in Food Control, 111 (2020),
https://doi.org/10.1016/j.foodcont.2019.107076 . .

TY  - JOUR
AU  - Bjelogrlić, Snežana
AU  - Todorović, Tamara R.
AU  - Kojić, Milan
AU  - Sencanski, Milan
AU  - Nikolić, Milan
AU  - Visnjevac, Aleksandar
AU  - Araskov, Jovana
AU  - Miljković, Marija
AU  - Muller, Christian D.
AU  - Filipović, Nenad
PY  - 2019
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/4916
AB  - Anticancer activity of Pd complexes 1-5 with bidentate N-heteroaromatic hydrazone ligands was investigated on human acute monocytic leukemia (THP-1; cells in a suspension) and human mammary adenocarcinoma (MCF-7; two-dimensional layer and three-dimensional spheroid tumor model) cell lines. For the Pd(II) complexes with condensation products of ethyl hydrazainoacetate and quinoline-8-carboxaldehyde (complex 1) and 2-for-mylpyridine (complex 3), for which apoptosis was determined as a mechanism of anticancer activity, further investigation revealed that they arrest the cell cycle in G0/G1 phase, induce generation of reactive oxygen species and inhibit Topoisomerase I in vitro. In silico studies corroborate experimental findings that these complexes show topoisomerase inhibition activity in the micromolar range and indicate binding to a DNA's minor groove as another potential target. Based on the results obtained by circular dichroism and fluorescence spectroscopy measurements, the most active complexes are suitable to be delivered to a blood stream via human serum albumin.
PB  - Elsevier Science Inc, New York
T2  - Journal of Inorganic Biochemistry
T1  - Pd(II) complexes with N-heteroaromatic hydrazone ligands: Anticancer activity, in silico and experimental target identification
VL  - 199
DO  - 10.1016/j.jinorgbio.2019.110758
ER  - 

@article{
author = "Bjelogrlić, Snežana and Todorović, Tamara R. and Kojić, Milan and Sencanski, Milan and Nikolić, Milan and Visnjevac, Aleksandar and Araskov, Jovana and Miljković, Marija and Muller, Christian D. and Filipović, Nenad",
year = "2019",
abstract = "Anticancer activity of Pd complexes 1-5 with bidentate N-heteroaromatic hydrazone ligands was investigated on human acute monocytic leukemia (THP-1; cells in a suspension) and human mammary adenocarcinoma (MCF-7; two-dimensional layer and three-dimensional spheroid tumor model) cell lines. For the Pd(II) complexes with condensation products of ethyl hydrazainoacetate and quinoline-8-carboxaldehyde (complex 1) and 2-for-mylpyridine (complex 3), for which apoptosis was determined as a mechanism of anticancer activity, further investigation revealed that they arrest the cell cycle in G0/G1 phase, induce generation of reactive oxygen species and inhibit Topoisomerase I in vitro. In silico studies corroborate experimental findings that these complexes show topoisomerase inhibition activity in the micromolar range and indicate binding to a DNA's minor groove as another potential target. Based on the results obtained by circular dichroism and fluorescence spectroscopy measurements, the most active complexes are suitable to be delivered to a blood stream via human serum albumin.",
publisher = "Elsevier Science Inc, New York",
journal = "Journal of Inorganic Biochemistry",
title = "Pd(II) complexes with N-heteroaromatic hydrazone ligands: Anticancer activity, in silico and experimental target identification",
volume = "199",
doi = "10.1016/j.jinorgbio.2019.110758"
}

Bjelogrlić, S., Todorović, T. R., Kojić, M., Sencanski, M., Nikolić, M., Visnjevac, A., Araskov, J., Miljković, M., Muller, C. D.,& Filipović, N.. (2019). Pd(II) complexes with N-heteroaromatic hydrazone ligands: Anticancer activity, in silico and experimental target identification. in Journal of Inorganic Biochemistry
Elsevier Science Inc, New York., 199.
https://doi.org/10.1016/j.jinorgbio.2019.110758

Bjelogrlić S, Todorović TR, Kojić M, Sencanski M, Nikolić M, Visnjevac A, Araskov J, Miljković M, Muller CD, Filipović N. Pd(II) complexes with N-heteroaromatic hydrazone ligands: Anticancer activity, in silico and experimental target identification. in Journal of Inorganic Biochemistry. 2019;199.
doi:10.1016/j.jinorgbio.2019.110758 .

Bjelogrlić, Snežana, Todorović, Tamara R., Kojić, Milan, Sencanski, Milan, Nikolić, Milan, Visnjevac, Aleksandar, Araskov, Jovana, Miljković, Marija, Muller, Christian D., Filipović, Nenad, "Pd(II) complexes with N-heteroaromatic hydrazone ligands: Anticancer activity, in silico and experimental target identification" in Journal of Inorganic Biochemistry, 199 (2019),
https://doi.org/10.1016/j.jinorgbio.2019.110758 . .

TY  - JOUR
AU  - Mirković, Nemanja
AU  - Polović, Natalija
AU  - Vukotić, Goran
AU  - Jovcić, Branko
AU  - Miljković, Marija
AU  - Radulović, Zorica
AU  - Diep, Dzung B.
AU  - Kojić, Milan
PY  - 2016
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/4208
AB  - Bacteriocin producers normally possess dedicated immunity systems to protect themselves from their own bacteriocins. Lactococcus lactis strains LMG2081 and BGBM50 are known as lactococcin G producers. However, BGBM50 was sensitive to LMG2081, which indicated that LMG2081 might produce additional bacteriocins that are not present in BGBM50. Therefore, whole-genome sequencing of the two strains was performed, and a lantibiotic operon (called lctLMG) was identified in LMG2081 but not in BGBM50. The lctLMG operon contains six open reading frames; the first three genes, lmgA, lmgM, and lmgT, are involved in the biosynthesis and export of bacteriocin, while the other three genes, lmgF, lmgE, and lmgG, are involved in lantibiotic immunity. Mutational analysis confirmed that the lctLMG operon is responsible for the additional antimicrobial activity. Specifically, site-directed mutation within this operon rendered LMG2081 inactive toward BGBM50. Subsequent purification and electrospray ionization-time of flight mass spectrometric analysis confirmed that the lantibiotic bacteriocin called lacticin LMG is exported as a 25-amino-acid peptide. Lacticin LMG is highly similar to the lacticin 481 group. It is interesting that a bacteriocin producer produces two different classes of bacteriocins, whose operons are located in the chromosome and a plasmid.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic
EP  - 2562
IS  - 8
SP  - 2555
VL  - 82
DO  - 10.1128/AEM.03988-15
ER  - 

@article{
author = "Mirković, Nemanja and Polović, Natalija and Vukotić, Goran and Jovcić, Branko and Miljković, Marija and Radulović, Zorica and Diep, Dzung B. and Kojić, Milan",
year = "2016",
abstract = "Bacteriocin producers normally possess dedicated immunity systems to protect themselves from their own bacteriocins. Lactococcus lactis strains LMG2081 and BGBM50 are known as lactococcin G producers. However, BGBM50 was sensitive to LMG2081, which indicated that LMG2081 might produce additional bacteriocins that are not present in BGBM50. Therefore, whole-genome sequencing of the two strains was performed, and a lantibiotic operon (called lctLMG) was identified in LMG2081 but not in BGBM50. The lctLMG operon contains six open reading frames; the first three genes, lmgA, lmgM, and lmgT, are involved in the biosynthesis and export of bacteriocin, while the other three genes, lmgF, lmgE, and lmgG, are involved in lantibiotic immunity. Mutational analysis confirmed that the lctLMG operon is responsible for the additional antimicrobial activity. Specifically, site-directed mutation within this operon rendered LMG2081 inactive toward BGBM50. Subsequent purification and electrospray ionization-time of flight mass spectrometric analysis confirmed that the lantibiotic bacteriocin called lacticin LMG is exported as a 25-amino-acid peptide. Lacticin LMG is highly similar to the lacticin 481 group. It is interesting that a bacteriocin producer produces two different classes of bacteriocins, whose operons are located in the chromosome and a plasmid.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic",
pages = "2562-2555",
number = "8",
volume = "82",
doi = "10.1128/AEM.03988-15"
}

Mirković, N., Polović, N., Vukotić, G., Jovcić, B., Miljković, M., Radulović, Z., Diep, D. B.,& Kojić, M.. (2016). Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 82(8), 2555-2562.
https://doi.org/10.1128/AEM.03988-15

Mirković N, Polović N, Vukotić G, Jovcić B, Miljković M, Radulović Z, Diep DB, Kojić M. Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic. in Applied and Environmental Microbiology. 2016;82(8):2555-2562.
doi:10.1128/AEM.03988-15 .

Mirković, Nemanja, Polović, Natalija, Vukotić, Goran, Jovcić, Branko, Miljković, Marija, Radulović, Zorica, Diep, Dzung B., Kojić, Milan, "Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic" in Applied and Environmental Microbiology, 82, no. 8 (2016):2555-2562,
https://doi.org/10.1128/AEM.03988-15 . .

TY  - JOUR
AU  - Miljković, Marija
AU  - Uzelac, Gordana
AU  - Mirković, Nemanja
AU  - Devescovi, Giulia
AU  - Diep, Dzung B.
AU  - Venturi, Vittorio
AU  - Kojić, Milan
PY  - 2016
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/4029
AB  - The Zn-dependent membrane-located protease YvjB has previously been shown to serve as a target receptor for LsbB, a class II leaderless lactococcal bacteriocin. Although yvjB is highly conserved in the genus Lactococcus, the bacteriocin appears to be active only against the subspecies L. lactis subsp. lactis. Comparative analysis of the YvjB proteins of a sensitive strain (YvjB(MN)) and a resistant strain (YvjB(MG)) showed that they differ from each other in 31 positions. In this study, we applied site-directed mutagenesis and performed directed binding studies to provide biochemical evidence that LsbB interacts with the third transmembrane helix of YvjB in susceptible cells. The site-directed mutagenesis of LsbB and YvjB proteins showed that certain amino acids and the length of LsbB are responsible for the bacteriocin activity, most probably through adequate interaction of these two proteins; the essential amino acids in LsbB responsible for the activity are tryptophan (Trp(25)) and terminal alanine (Ala(30)). It was also shown that the distance between Trp(25) and terminal alanine is crucial for LsbB activity. The crucial region in YvjB for the interaction with LsbB is the beginning of the third transmembrane helix, particularly amino acids tyrosine (Tyr(356)) and alanine (Ala(353)). In vitro experiments showed that LsbB could interact with both YvjB(MN) and YvjB(MG), but the strength of interaction is significantly less with YvjB(MG). In vivo experiments with immunofluorescently labeled antibody demonstrated that LsbB specifically interacts only with cells carrying YvjB(MN). IMPORTANCE The antimicrobial activity of LsbB bacteriocin depends on the correct interaction with the corresponding receptor in the bacterial membrane of sensitive cells. Membrane-located bacteriocin receptors have essential primary functions, such as cell wall synthesis or sugar transport, and it seems that interaction with bacteriocins is suicidal for cells. This study showed that the C-terminal part of LsbB is crucial for the bacteriocin activity, most probably through adequate interaction with the third transmembrane domain of the YvjB receptor. The conserved Tyr(356) and Ala(353) residues of YvjB are essential for the function of this Zn-dependent membrane-located protease as a bacteriocin receptor.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor
EP  - 5374
IS  - 17
SP  - 5364
VL  - 82
DO  - 10.1128/AEM.01293-16
ER  - 

@article{
author = "Miljković, Marija and Uzelac, Gordana and Mirković, Nemanja and Devescovi, Giulia and Diep, Dzung B. and Venturi, Vittorio and Kojić, Milan",
year = "2016",
abstract = "The Zn-dependent membrane-located protease YvjB has previously been shown to serve as a target receptor for LsbB, a class II leaderless lactococcal bacteriocin. Although yvjB is highly conserved in the genus Lactococcus, the bacteriocin appears to be active only against the subspecies L. lactis subsp. lactis. Comparative analysis of the YvjB proteins of a sensitive strain (YvjB(MN)) and a resistant strain (YvjB(MG)) showed that they differ from each other in 31 positions. In this study, we applied site-directed mutagenesis and performed directed binding studies to provide biochemical evidence that LsbB interacts with the third transmembrane helix of YvjB in susceptible cells. The site-directed mutagenesis of LsbB and YvjB proteins showed that certain amino acids and the length of LsbB are responsible for the bacteriocin activity, most probably through adequate interaction of these two proteins; the essential amino acids in LsbB responsible for the activity are tryptophan (Trp(25)) and terminal alanine (Ala(30)). It was also shown that the distance between Trp(25) and terminal alanine is crucial for LsbB activity. The crucial region in YvjB for the interaction with LsbB is the beginning of the third transmembrane helix, particularly amino acids tyrosine (Tyr(356)) and alanine (Ala(353)). In vitro experiments showed that LsbB could interact with both YvjB(MN) and YvjB(MG), but the strength of interaction is significantly less with YvjB(MG). In vivo experiments with immunofluorescently labeled antibody demonstrated that LsbB specifically interacts only with cells carrying YvjB(MN). IMPORTANCE The antimicrobial activity of LsbB bacteriocin depends on the correct interaction with the corresponding receptor in the bacterial membrane of sensitive cells. Membrane-located bacteriocin receptors have essential primary functions, such as cell wall synthesis or sugar transport, and it seems that interaction with bacteriocins is suicidal for cells. This study showed that the C-terminal part of LsbB is crucial for the bacteriocin activity, most probably through adequate interaction with the third transmembrane domain of the YvjB receptor. The conserved Tyr(356) and Ala(353) residues of YvjB are essential for the function of this Zn-dependent membrane-located protease as a bacteriocin receptor.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor",
pages = "5374-5364",
number = "17",
volume = "82",
doi = "10.1128/AEM.01293-16"
}

Miljković, M., Uzelac, G., Mirković, N., Devescovi, G., Diep, D. B., Venturi, V.,& Kojić, M.. (2016). LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 82(17), 5364-5374.
https://doi.org/10.1128/AEM.01293-16

Miljković M, Uzelac G, Mirković N, Devescovi G, Diep DB, Venturi V, Kojić M. LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor. in Applied and Environmental Microbiology. 2016;82(17):5364-5374.
doi:10.1128/AEM.01293-16 .

Miljković, Marija, Uzelac, Gordana, Mirković, Nemanja, Devescovi, Giulia, Diep, Dzung B., Venturi, Vittorio, Kojić, Milan, "LsbB Bacteriocin Interacts with the Third Transmembrane Domain of the YvjB Receptor" in Applied and Environmental Microbiology, 82, no. 17 (2016):5364-5374,
https://doi.org/10.1128/AEM.01293-16 . .

TY  - JOUR
AU  - Uzelac, Gordana
AU  - Miljković, Marija
AU  - Lozo, Jelena
AU  - Radulović, Zorica
AU  - Tosić, Nataša
AU  - Kojić, Milan
PY  - 2015
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/3689
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 Tosić, 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., Tosić, 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, Tosić 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, Tosić, 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  - Vukotić, Goran
AU  - Mirković, Nemanja
AU  - Jovcić, Branko
AU  - Miljković, Marija
AU  - Strahinić, Ivana
AU  - Fira, Djordje
AU  - Radulović, Zorica
AU  - Kojić, Milan
PY  - 2015
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/3817
AB  - Proteinases and bacteriocins are of great importance to the dairy industry, but their interactions have not been studied so far. Lactococcus lactis subsp. lactis BGMN1-5 is a natural isolate from homemade semi-hard cheese which produces two bacteriocins (Lactococcin B and LsbB), as well as proteinase PrtP. A medium-dependent increase in the bacteriocin LcnB activity of L. lactis BGMN1-501, a derivate of L. lactis subsp. lactis BGMN1-5, was shown to be accompanied by a decrease in its promoter activity. A similar effect of media components on gene expression was reported for proteinase PrtP whose gene is co-localized on the same plasmid as the IcnB gene. Thus, the PrtP-LcnB interplay was investigated. Single gene knockout mutants were constructed with disrupted prtP or IcnB genes. PrtP mutants showed higher bacteriocin activity that had lost its growth medium dependence, which was in contrast to the original strain. When LcnB from this mutant was combined with proteinase from the LonB(-) mutant in vitro, its activity was rendered to the original level, suggesting that proteinase reduces bacteriocin activity. We propose a new model of medium dependent expression of these genes with regard to the effects of their interaction in vivo.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation
VL  - 6
DO  - 10.3389/fmicb.2015.00092
ER  - 

@article{
author = "Vukotić, Goran and Mirković, Nemanja and Jovcić, Branko and Miljković, Marija and Strahinić, Ivana and Fira, Djordje and Radulović, Zorica and Kojić, Milan",
year = "2015",
abstract = "Proteinases and bacteriocins are of great importance to the dairy industry, but their interactions have not been studied so far. Lactococcus lactis subsp. lactis BGMN1-5 is a natural isolate from homemade semi-hard cheese which produces two bacteriocins (Lactococcin B and LsbB), as well as proteinase PrtP. A medium-dependent increase in the bacteriocin LcnB activity of L. lactis BGMN1-501, a derivate of L. lactis subsp. lactis BGMN1-5, was shown to be accompanied by a decrease in its promoter activity. A similar effect of media components on gene expression was reported for proteinase PrtP whose gene is co-localized on the same plasmid as the IcnB gene. Thus, the PrtP-LcnB interplay was investigated. Single gene knockout mutants were constructed with disrupted prtP or IcnB genes. PrtP mutants showed higher bacteriocin activity that had lost its growth medium dependence, which was in contrast to the original strain. When LcnB from this mutant was combined with proteinase from the LonB(-) mutant in vitro, its activity was rendered to the original level, suggesting that proteinase reduces bacteriocin activity. We propose a new model of medium dependent expression of these genes with regard to the effects of their interaction in vivo.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation",
volume = "6",
doi = "10.3389/fmicb.2015.00092"
}

Vukotić, G., Mirković, N., Jovcić, B., Miljković, M., Strahinić, I., Fira, D., Radulović, Z.,& Kojić, M.. (2015). Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation. in Frontiers in Microbiology
Frontiers Media Sa, Lausanne., 6.
https://doi.org/10.3389/fmicb.2015.00092

Vukotić G, Mirković N, Jovcić B, Miljković M, Strahinić I, Fira D, Radulović Z, Kojić M. Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation. in Frontiers in Microbiology. 2015;6.
doi:10.3389/fmicb.2015.00092 .

Vukotić, Goran, Mirković, Nemanja, Jovcić, Branko, Miljković, Marija, Strahinić, Ivana, Fira, Djordje, Radulović, Zorica, Kojić, Milan, "Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation" in Frontiers in Microbiology, 6 (2015),
https://doi.org/10.3389/fmicb.2015.00092 . .