Radulović, Zorica

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  • Radulović, Zorica (4)
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Author's Bibliography

Lactococcus lactis LMG2081 Produces Two Bacteriocins, a Nonlantibiotic and a Novel Lantibiotic

Mirković, Nemanja; Polović, Natalija; Vukotić, Goran; Jovčić, Branko; Miljković, Marija; Radulović, Zorica; Diep, Dzung B.; Kojić, Milan

(Amer Soc Microbiology, Washington, 2016)

TY  - JOUR
AU  - Mirković, Nemanja
AU  - Polović, Natalija
AU  - Vukotić, Goran
AU  - Jovčić, Branko
AU  - Miljković, Marija
AU  - Radulović, Zorica
AU  - Diep, Dzung B.
AU  - Kojić, Milan
PY  - 2016
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/980
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 Jovčić, 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., Jovčić, 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, Jovčić 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, Jovčić, 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 . .
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Isolation and Characterisation of Bacteriocin and Aggregation-Promoting Factor Production in Lactococcus lactis ssp lactis BGBM50 Strain

Mirković, Nemanja; Radulović, Zorica; Uzelac, Gordana; Lozo, Jelena; Obradović, Dragojlo; Topisirović, Ljubiša; Kojić, Milan

(University of Zagreb, 2015)

TY  - JOUR
AU  - Mirković, Nemanja
AU  - Radulović, Zorica
AU  - Uzelac, Gordana
AU  - Lozo, Jelena
AU  - Obradović, Dragojlo
AU  - Topisirović, Ljubiša
AU  - Kojić, Milan
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/870
AB  - Lactococcus locus ssp. lactis BGBM50, a producer of lactococcin G and aggregation-promoting factor, was isolated from selected lactic acid bacteria taken from semi-hard cheese traditionally produced in the village Zanjic, Montenegro. Strain BGBM50 harbours a number of plasmids of different sizes. Plasmid curing experiments showed that genes for bacteriocin production are located on pBM140, a plasmid 140 kb in length. PCR analysis with primers specific for lactococcin Q and G genes gave fragment of the expected size. In addition, after plasmid curing of strain BGBM50, different derivatives with altered phenotypes were obtained, among them BGBM50-34 strain, which retained bacteriocin synthesis but had enhanced aggregation ability.
PB  - University of Zagreb
T2  - Food Technology and Biotechnology
T1  - Isolation and Characterisation of Bacteriocin and Aggregation-Promoting Factor Production in Lactococcus lactis ssp lactis BGBM50 Strain
EP  - 242
IS  - 2
SP  - 237
VL  - 53
DO  - 10.17113/ftb.53.02.15.3846
ER  - 
@article{
author = "Mirković, Nemanja and Radulović, Zorica and Uzelac, Gordana and Lozo, Jelena and Obradović, Dragojlo and Topisirović, Ljubiša and Kojić, Milan",
year = "2015",
abstract = "Lactococcus locus ssp. lactis BGBM50, a producer of lactococcin G and aggregation-promoting factor, was isolated from selected lactic acid bacteria taken from semi-hard cheese traditionally produced in the village Zanjic, Montenegro. Strain BGBM50 harbours a number of plasmids of different sizes. Plasmid curing experiments showed that genes for bacteriocin production are located on pBM140, a plasmid 140 kb in length. PCR analysis with primers specific for lactococcin Q and G genes gave fragment of the expected size. In addition, after plasmid curing of strain BGBM50, different derivatives with altered phenotypes were obtained, among them BGBM50-34 strain, which retained bacteriocin synthesis but had enhanced aggregation ability.",
publisher = "University of Zagreb",
journal = "Food Technology and Biotechnology",
title = "Isolation and Characterisation of Bacteriocin and Aggregation-Promoting Factor Production in Lactococcus lactis ssp lactis BGBM50 Strain",
pages = "242-237",
number = "2",
volume = "53",
doi = "10.17113/ftb.53.02.15.3846"
}
Mirković, N., Radulović, Z., Uzelac, G., Lozo, J., Obradović, D., Topisirović, L.,& Kojić, M.. (2015). Isolation and Characterisation of Bacteriocin and Aggregation-Promoting Factor Production in Lactococcus lactis ssp lactis BGBM50 Strain. in Food Technology and Biotechnology
University of Zagreb., 53(2), 237-242.
https://doi.org/10.17113/ftb.53.02.15.3846
Mirković N, Radulović Z, Uzelac G, Lozo J, Obradović D, Topisirović L, Kojić M. Isolation and Characterisation of Bacteriocin and Aggregation-Promoting Factor Production in Lactococcus lactis ssp lactis BGBM50 Strain. in Food Technology and Biotechnology. 2015;53(2):237-242.
doi:10.17113/ftb.53.02.15.3846 .
Mirković, Nemanja, Radulović, Zorica, Uzelac, Gordana, Lozo, Jelena, Obradović, Dragojlo, Topisirović, Ljubiša, Kojić, Milan, "Isolation and Characterisation of Bacteriocin and Aggregation-Promoting Factor Production in Lactococcus lactis ssp lactis BGBM50 Strain" in Food Technology and Biotechnology, 53, no. 2 (2015):237-242,
https://doi.org/10.17113/ftb.53.02.15.3846 . .
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Proteinase PrtP impairs lactococcin LcnB activity in Lactococcus lactis BGMN1-501: new insights into bacteriocin regulation

Vukotić, Goran; Mirković, Nemanja; Jovčić, Branko; Miljković, Marija; Strahinić, Ivana; Fira, Đorđe; Radulović, Zorica; Kojić, Milan

(Frontiers Media Sa, Lausanne, 2015)

TY  - JOUR
AU  - Vukotić, Goran
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Miljković, Marija
AU  - Strahinić, Ivana
AU  - Fira, Đorđe
AU  - Radulović, Zorica
AU  - Kojić, Milan
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/895
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 Jovčić, Branko and Miljković, Marija and Strahinić, Ivana and Fira, Đorđe 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., Jovčić, B., Miljković, M., Strahinić, I., Fira, Đ., 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, Jovčić B, Miljković M, Strahinić I, Fira Đ, 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, Jovčić, Branko, Miljković, Marija, Strahinić, Ivana, Fira, Đorđe, 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 . .
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Expression of bacteriocin LsbB is dependent on a transcription terminator

Uzelac, Gordana; Miljković, Marija; Lozo, Jelena; Radulović, Zorica; Tošić, Nataša; Kojić, Milan

(Elsevier Gmbh, Urban & Fischer Verlag, Jena, 2015)

TY  - JOUR
AU  - Uzelac, Gordana
AU  - Miljković, Marija
AU  - Lozo, Jelena
AU  - Radulović, Zorica
AU  - Tošić, Nataša
AU  - Kojić, Milan
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/829
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 . .
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