TY  - JOUR
AU  - Vukotić, Goran
AU  - Polović, Natalija
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Stanisavljević, Nemanja
AU  - Fira, Đorđe
AU  - Kojić, Milan
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1251
AB  - In our previous study we demonstrated that proteinase PrtP is able to impair bacteriocin LcnB activity, despite being produced by the same organism and encoded by the same plasmid. However, precise mechanism of this action, i.e., the exact cleavage site within LcnB bacteriocin, as well as its effect on antimicrobial activity of the resulting peptide remained vague. Here we further explored the interplay between these two proteins and defined, using mass spectrometry, that this unusual hydrolysis indeed occurs in vivo, between the sixth and seventh amino acid on the N terminus of LcnB. To address whether the cleaved form of LcnB retains any level of activity, both recombinant and chemically synthesized variant of truncated LcnB were engineered and produced, but demonstrated no antimicrobial activity. When LcnB was recombinantly overexpressed and subjected to PrtP digestion, the change in its antimicrobial activity was monitored and the degradation products analyzed with reverse-phase high-pressure liquid chromatography. The results confirmed the inactivity of the truncated LcnB and additionally corroborated the PrtP cleavage site in LcnB bacteriocin. In addition, it was demonstrated that, once truncated, LcnB is not able to bind its receptor and is susceptible to additional hydrolysis. This is the first report on proteolytic inactivation of bacteriocins inside the same bacterial host.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. lactis BGMN1-501
VL  - 10
DO  - 10.3389/fmicb.2019.00874
ER  - 

@article{
author = "Vukotić, Goran and Polović, Natalija and Mirković, Nemanja and Jovčić, Branko and Stanisavljević, Nemanja and Fira, Đorđe and Kojić, Milan",
year = "2019",
abstract = "In our previous study we demonstrated that proteinase PrtP is able to impair bacteriocin LcnB activity, despite being produced by the same organism and encoded by the same plasmid. However, precise mechanism of this action, i.e., the exact cleavage site within LcnB bacteriocin, as well as its effect on antimicrobial activity of the resulting peptide remained vague. Here we further explored the interplay between these two proteins and defined, using mass spectrometry, that this unusual hydrolysis indeed occurs in vivo, between the sixth and seventh amino acid on the N terminus of LcnB. To address whether the cleaved form of LcnB retains any level of activity, both recombinant and chemically synthesized variant of truncated LcnB were engineered and produced, but demonstrated no antimicrobial activity. When LcnB was recombinantly overexpressed and subjected to PrtP digestion, the change in its antimicrobial activity was monitored and the degradation products analyzed with reverse-phase high-pressure liquid chromatography. The results confirmed the inactivity of the truncated LcnB and additionally corroborated the PrtP cleavage site in LcnB bacteriocin. In addition, it was demonstrated that, once truncated, LcnB is not able to bind its receptor and is susceptible to additional hydrolysis. This is the first report on proteolytic inactivation of bacteriocins inside the same bacterial host.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. lactis BGMN1-501",
volume = "10",
doi = "10.3389/fmicb.2019.00874"
}

Vukotić, G., Polović, N., Mirković, N., Jovčić, B., Stanisavljević, N., Fira, Đ.,& Kojić, M.. (2019). Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. lactis BGMN1-501. in Frontiers in Microbiology
Frontiers Media Sa, Lausanne., 10.
https://doi.org/10.3389/fmicb.2019.00874

Vukotić G, Polović N, Mirković N, Jovčić B, Stanisavljević N, Fira Đ, Kojić M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. lactis BGMN1-501. in Frontiers in Microbiology. 2019;10.
doi:10.3389/fmicb.2019.00874 .

Vukotić, Goran, Polović, Natalija, Mirković, Nemanja, Jovčić, Branko, Stanisavljević, Nemanja, Fira, Đorđe, Kojić, Milan, "Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. lactis BGMN1-501" in Frontiers in Microbiology, 10 (2019),
https://doi.org/10.3389/fmicb.2019.00874 . .

TY  - JOUR
AU  - Vukotić, Goran
AU  - Strahinić, Ivana
AU  - Begović, Jelena
AU  - Lukić, Jovanka
AU  - Kojić, Milan
AU  - Fira, Đorđe
PY  - 2016
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/992
AB  - Lactocepins or CEPs are large cell wall bound extracellular proteinases of lactic acid bacteria, involved in protein breakdown and utilization. They are responsible for many health-promoting traits of food products fermented with these organisms, but also essential for probiotic effects of certain strains. Different mesophilic strains selected within the species Lactobacillus zeae, Lb. casei, Lb. rhamnosus, and Lb. plantarum were analyzed for their proteolytic activity towards main fractions of milk proteins-caseins and whey proteins. The strains showing excellent proteolytic features were further examined for presence of corresponding proteinase gene(s). It was found that Lb. zeae LMG17315 possessed catalytic domains of three distinct proteinase genes, unique feature in Lb. casei group, which are similar but not identical to previously characterized prtP and prtR genes. Lb. casei neotype strain ATCC393 was also analysed and based on obtained results its reclassification in taxon Lb. zeae is supported. In addition, we report catalytic domain of prtR-type gene in Lb. plantarum LMG9208, which is first such report in this species, and it is first time that this gene is reported outside Lb. casei group.
PB  - Maik Nauka/Interperiodica/Springer, New York
T2  - Microbiology
T1  - Survey on proteolytic activity and diversity of proteinase genes in mesophilic lactobacilli
EP  - 41
IS  - 1
SP  - 33
VL  - 85
DO  - 10.1134/S002626171601015X
ER  - 

@article{
author = "Vukotić, Goran and Strahinić, Ivana and Begović, Jelena and Lukić, Jovanka and Kojić, Milan and Fira, Đorđe",
year = "2016",
abstract = "Lactocepins or CEPs are large cell wall bound extracellular proteinases of lactic acid bacteria, involved in protein breakdown and utilization. They are responsible for many health-promoting traits of food products fermented with these organisms, but also essential for probiotic effects of certain strains. Different mesophilic strains selected within the species Lactobacillus zeae, Lb. casei, Lb. rhamnosus, and Lb. plantarum were analyzed for their proteolytic activity towards main fractions of milk proteins-caseins and whey proteins. The strains showing excellent proteolytic features were further examined for presence of corresponding proteinase gene(s). It was found that Lb. zeae LMG17315 possessed catalytic domains of three distinct proteinase genes, unique feature in Lb. casei group, which are similar but not identical to previously characterized prtP and prtR genes. Lb. casei neotype strain ATCC393 was also analysed and based on obtained results its reclassification in taxon Lb. zeae is supported. In addition, we report catalytic domain of prtR-type gene in Lb. plantarum LMG9208, which is first such report in this species, and it is first time that this gene is reported outside Lb. casei group.",
publisher = "Maik Nauka/Interperiodica/Springer, New York",
journal = "Microbiology",
title = "Survey on proteolytic activity and diversity of proteinase genes in mesophilic lactobacilli",
pages = "41-33",
number = "1",
volume = "85",
doi = "10.1134/S002626171601015X"
}

Vukotić, G., Strahinić, I., Begović, J., Lukić, J., Kojić, M.,& Fira, Đ.. (2016). Survey on proteolytic activity and diversity of proteinase genes in mesophilic lactobacilli. in Microbiology
Maik Nauka/Interperiodica/Springer, New York., 85(1), 33-41.
https://doi.org/10.1134/S002626171601015X

Vukotić G, Strahinić I, Begović J, Lukić J, Kojić M, Fira Đ. Survey on proteolytic activity and diversity of proteinase genes in mesophilic lactobacilli. in Microbiology. 2016;85(1):33-41.
doi:10.1134/S002626171601015X .

Vukotić, Goran, Strahinić, Ivana, Begović, Jelena, Lukić, Jovanka, Kojić, Milan, Fira, Đorđe, "Survey on proteolytic activity and diversity of proteinase genes in mesophilic lactobacilli" in Microbiology, 85, no. 1 (2016):33-41,
https://doi.org/10.1134/S002626171601015X . .

TY  - JOUR
AU  - Cirković, Ivana
AU  - Bozić, Dragana D.
AU  - Draganić, Veselin
AU  - Lozo, Jelena
AU  - Berić, Tanja
AU  - Kojić, Milan
AU  - Arsić, Biljana
AU  - Garalejić, Eliana
AU  - Đukić, Slobodanka
AU  - Stanković, Slaviša
PY  - 2016
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/958
AB  - Background Coagulase negative staphylococci (CoNS) and Listeria monocytogenes have important roles in pathogenesis of various genital tract infections and fatal foetomaternal infections, respectively. The aim of our study was to investigate the inhibitory effects of two novel bacteriocins on biofilms of CoNS and L. monocytogenes genital isolates. Methods The effects of licheniocin 50.2 from Bacillus licheniformis VPS50.2 and crude extract of bacteriocins produced by Lactococcus lactis subsp. lactis biovar. diacetylactis BGBU1-4 (BGBU1-4 crude extract) were evaluated on biofilm formation and formed biofilms of eight CoNS (four S. epidermidis, two S. hominis, one S. lugdunensis and one S. haemolyticus) and 12 L. monocytogenes genital isolates. Results Licheniocin 50.2 and BGBU1-4 crude extract inhibited the growth of both CoNS and L. monocytogenes isolates, with MIC values in the range between 200-400 AU/ml for licheniocin 50.2 and 400-3200 AU/ml for BGBU1-4 crude extract. Subinhibitory concentrations (1/2 x and 1/4 x MIC) of licheniocin 50.2 inhibited biofilm formation by all CoNS isolates (p  lt  0.05, respectively), while BGBU1-4 crude extract inhibited biofilm formation by all L. monocytogenes isolates (p  lt  0.01 and p  lt  0.05, respectively). Both bacteriocins in concentrations of 100 AU/mL and 200 AU/mL reduced the amount of 24 h old CoNS and L. monocytogenes biofilms (p  lt  0.05, p  lt  0.01, p  lt  0.001). Conclusions This study suggests that novel bacteriocins have potential to be used for genital application, to prevent biofilm formation and/or to eradicate formed biofilms, and consequently reduce genital and neonatal infections by CoNS and L. monocytogenes.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - Licheniocin 50.2 and Bacteriocins from Lactococcus lactis subsp lactis biovar. diacetylactis BGBU1-4 Inhibit Biofilms of Coagulase Negative Staphylococci and Listeria monocytogenes Clinical Isolates
IS  - 12
VL  - 11
DO  - 10.1371/journal.pone.0167995
ER  - 

@article{
author = "Cirković, Ivana and Bozić, Dragana D. and Draganić, Veselin and Lozo, Jelena and Berić, Tanja and Kojić, Milan and Arsić, Biljana and Garalejić, Eliana and Đukić, Slobodanka and Stanković, Slaviša",
year = "2016",
abstract = "Background Coagulase negative staphylococci (CoNS) and Listeria monocytogenes have important roles in pathogenesis of various genital tract infections and fatal foetomaternal infections, respectively. The aim of our study was to investigate the inhibitory effects of two novel bacteriocins on biofilms of CoNS and L. monocytogenes genital isolates. Methods The effects of licheniocin 50.2 from Bacillus licheniformis VPS50.2 and crude extract of bacteriocins produced by Lactococcus lactis subsp. lactis biovar. diacetylactis BGBU1-4 (BGBU1-4 crude extract) were evaluated on biofilm formation and formed biofilms of eight CoNS (four S. epidermidis, two S. hominis, one S. lugdunensis and one S. haemolyticus) and 12 L. monocytogenes genital isolates. Results Licheniocin 50.2 and BGBU1-4 crude extract inhibited the growth of both CoNS and L. monocytogenes isolates, with MIC values in the range between 200-400 AU/ml for licheniocin 50.2 and 400-3200 AU/ml for BGBU1-4 crude extract. Subinhibitory concentrations (1/2 x and 1/4 x MIC) of licheniocin 50.2 inhibited biofilm formation by all CoNS isolates (p  lt  0.05, respectively), while BGBU1-4 crude extract inhibited biofilm formation by all L. monocytogenes isolates (p  lt  0.01 and p  lt  0.05, respectively). Both bacteriocins in concentrations of 100 AU/mL and 200 AU/mL reduced the amount of 24 h old CoNS and L. monocytogenes biofilms (p  lt  0.05, p  lt  0.01, p  lt  0.001). Conclusions This study suggests that novel bacteriocins have potential to be used for genital application, to prevent biofilm formation and/or to eradicate formed biofilms, and consequently reduce genital and neonatal infections by CoNS and L. monocytogenes.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "Licheniocin 50.2 and Bacteriocins from Lactococcus lactis subsp lactis biovar. diacetylactis BGBU1-4 Inhibit Biofilms of Coagulase Negative Staphylococci and Listeria monocytogenes Clinical Isolates",
number = "12",
volume = "11",
doi = "10.1371/journal.pone.0167995"
}

Cirković, I., Bozić, D. D., Draganić, V., Lozo, J., Berić, T., Kojić, M., Arsić, B., Garalejić, E., Đukić, S.,& Stanković, S.. (2016). Licheniocin 50.2 and Bacteriocins from Lactococcus lactis subsp lactis biovar. diacetylactis BGBU1-4 Inhibit Biofilms of Coagulase Negative Staphylococci and Listeria monocytogenes Clinical Isolates. in PLoS One
Public Library Science, San Francisco., 11(12).
https://doi.org/10.1371/journal.pone.0167995

Cirković I, Bozić DD, Draganić V, Lozo J, Berić T, Kojić M, Arsić B, Garalejić E, Đukić S, Stanković S. Licheniocin 50.2 and Bacteriocins from Lactococcus lactis subsp lactis biovar. diacetylactis BGBU1-4 Inhibit Biofilms of Coagulase Negative Staphylococci and Listeria monocytogenes Clinical Isolates. in PLoS One. 2016;11(12).
doi:10.1371/journal.pone.0167995 .

Cirković, Ivana, Bozić, Dragana D., Draganić, Veselin, Lozo, Jelena, Berić, Tanja, Kojić, Milan, Arsić, Biljana, Garalejić, Eliana, Đukić, Slobodanka, Stanković, Slaviša, "Licheniocin 50.2 and Bacteriocins from Lactococcus lactis subsp lactis biovar. diacetylactis BGBU1-4 Inhibit Biofilms of Coagulase Negative Staphylococci and Listeria monocytogenes Clinical Isolates" in PLoS One, 11, no. 12 (2016),
https://doi.org/10.1371/journal.pone.0167995 . .

TY  - JOUR
AU  - Stanisavljević, Nemanja
AU  - Vukotić, Goran 
AU  - Pastor, Ferenc T.
AU  - Suznjević, Desanka
AU  - Jovanović, Živko
AU  - Strahinić, Ivana
AU  - Fira, Đorđe
AU  - Radović, Svetlana S.
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/845
AB  - Nine Lactobacillus strains known for surface proteinase activity were chosen from our collection and tested for their ability to grow in pea seed protein-based medium, and to hydrolyze purified pea proteins in order to produce peptides with antioxidant (AO) activity. Two strains, Lactobacillus rhamnosus BGT10 and Lactobacillus zeae LMG17315, exhibited strong proteolytic activity against pea proteins. The AO activity of the pea hydrolysate fraction, MW  lt  10 kDa, obtained by the fermentation of purified pea proteins with Lactobacillus rhamnosus BGT10, was tested by standard spectrophotometric assays (DPPH, ABTS, Fe3+-reducing capacity) and the recently developed direct current (DC) polarographic assay. The low molecular weight fraction of the obtained hydrolysate was separated using ion exchange chromatography, while the AO activity of eluted fractions was determined by means of a sensitive DC polarographic assay without previous concentration of samples. Results revealed that the fraction present in low abundance that contained basic peptides possessed the highest antioxidant activity. Based on the obtained results, it can be concluded that Lactobacillus rhamnosus BGT10 should be further investigated as a candidate strain for large-scale production of bioactive peptides from legume proteins.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria
EP  - 1042
IS  - 3
SP  - 1033
VL  - 67
DO  - 10.2298/ABS150130066S
ER  - 

@article{
author = "Stanisavljević, Nemanja and Vukotić, Goran  and Pastor, Ferenc T. and Suznjević, Desanka and Jovanović, Živko and Strahinić, Ivana and Fira, Đorđe and Radović, Svetlana S.",
year = "2015",
abstract = "Nine Lactobacillus strains known for surface proteinase activity were chosen from our collection and tested for their ability to grow in pea seed protein-based medium, and to hydrolyze purified pea proteins in order to produce peptides with antioxidant (AO) activity. Two strains, Lactobacillus rhamnosus BGT10 and Lactobacillus zeae LMG17315, exhibited strong proteolytic activity against pea proteins. The AO activity of the pea hydrolysate fraction, MW  lt  10 kDa, obtained by the fermentation of purified pea proteins with Lactobacillus rhamnosus BGT10, was tested by standard spectrophotometric assays (DPPH, ABTS, Fe3+-reducing capacity) and the recently developed direct current (DC) polarographic assay. The low molecular weight fraction of the obtained hydrolysate was separated using ion exchange chromatography, while the AO activity of eluted fractions was determined by means of a sensitive DC polarographic assay without previous concentration of samples. Results revealed that the fraction present in low abundance that contained basic peptides possessed the highest antioxidant activity. Based on the obtained results, it can be concluded that Lactobacillus rhamnosus BGT10 should be further investigated as a candidate strain for large-scale production of bioactive peptides from legume proteins.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria",
pages = "1042-1033",
number = "3",
volume = "67",
doi = "10.2298/ABS150130066S"
}

Stanisavljević, N., Vukotić, G., Pastor, F. T., Suznjević, D., Jovanović, Ž., Strahinić, I., Fira, Đ.,& Radović, S. S.. (2015). Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 67(3), 1033-1042.
https://doi.org/10.2298/ABS150130066S

Stanisavljević N, Vukotić G, Pastor FT, Suznjević D, Jovanović Ž, Strahinić I, Fira Đ, Radović SS. Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria. in Archives of Biological Sciences. 2015;67(3):1033-1042.
doi:10.2298/ABS150130066S .

Stanisavljević, Nemanja, Vukotić, Goran , Pastor, Ferenc T., Suznjević, Desanka, Jovanović, Živko, Strahinić, Ivana, Fira, Đorđe, Radović, Svetlana S., "Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria" in Archives of Biological Sciences, 67, no. 3 (2015):1033-1042,
https://doi.org/10.2298/ABS150130066S . .

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 . .

TY  - JOUR
AU  - Ivanović, Zarko
AU  - Popović, Tatjana
AU  - Janse, Jaap
AU  - Kojić, Milan
AU  - Stanković, Slaviša
AU  - Gavrilović, Veljko
AU  - Fira, Đorđe
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/854
AB  - The purpose of the present study was to investigate the genetic diversity of X. arboricola pv. juglandis strains in Serbia. This bacterium is the causal agent of walnut blight and is also associated with apical necrosis of immature walnut fruits. Although walnut blight is long known and widespread in Serbia, a systematic strain diversity study of Xanthomonas arboricola pv. juglandis strains from different regions in Serbia has not been performed. The objectives of this work were to examine the molecular diversity and its possible biological significance of 59 isolates of X. arboricola pv. juglandis collected from different geographic locations in Serbia. Genomic variability was assessed by using repetitive PCR, SpeI macrorestriction analysis of genomic DNAs by pulsed-field gel electrophoresis (PFGE) and partial sequencing of the gyrB gene. Molecular analyses showed substantial genetic diversity among strains and existence of diverse populations of X. arboricola pv. juglandis in Serbia.
PB  - Springer, Dordrecht
T2  - European Journal of Plant Pathology
T1  - Molecular assessment of genetic diversity of Xanthomonas arboricola pv. juglandis strains from Serbia by various DNA fingerprinting techniques
EP  - 145
IS  - 1
SP  - 133
VL  - 141
DO  - 10.1007/s10658-014-0531-5
ER  - 

@article{
author = "Ivanović, Zarko and Popović, Tatjana and Janse, Jaap and Kojić, Milan and Stanković, Slaviša and Gavrilović, Veljko and Fira, Đorđe",
year = "2015",
abstract = "The purpose of the present study was to investigate the genetic diversity of X. arboricola pv. juglandis strains in Serbia. This bacterium is the causal agent of walnut blight and is also associated with apical necrosis of immature walnut fruits. Although walnut blight is long known and widespread in Serbia, a systematic strain diversity study of Xanthomonas arboricola pv. juglandis strains from different regions in Serbia has not been performed. The objectives of this work were to examine the molecular diversity and its possible biological significance of 59 isolates of X. arboricola pv. juglandis collected from different geographic locations in Serbia. Genomic variability was assessed by using repetitive PCR, SpeI macrorestriction analysis of genomic DNAs by pulsed-field gel electrophoresis (PFGE) and partial sequencing of the gyrB gene. Molecular analyses showed substantial genetic diversity among strains and existence of diverse populations of X. arboricola pv. juglandis in Serbia.",
publisher = "Springer, Dordrecht",
journal = "European Journal of Plant Pathology",
title = "Molecular assessment of genetic diversity of Xanthomonas arboricola pv. juglandis strains from Serbia by various DNA fingerprinting techniques",
pages = "145-133",
number = "1",
volume = "141",
doi = "10.1007/s10658-014-0531-5"
}

Ivanović, Z., Popović, T., Janse, J., Kojić, M., Stanković, S., Gavrilović, V.,& Fira, Đ.. (2015). Molecular assessment of genetic diversity of Xanthomonas arboricola pv. juglandis strains from Serbia by various DNA fingerprinting techniques. in European Journal of Plant Pathology
Springer, Dordrecht., 141(1), 133-145.
https://doi.org/10.1007/s10658-014-0531-5

Ivanović Z, Popović T, Janse J, Kojić M, Stanković S, Gavrilović V, Fira Đ. Molecular assessment of genetic diversity of Xanthomonas arboricola pv. juglandis strains from Serbia by various DNA fingerprinting techniques. in European Journal of Plant Pathology. 2015;141(1):133-145.
doi:10.1007/s10658-014-0531-5 .

Ivanović, Zarko, Popović, Tatjana, Janse, Jaap, Kojić, Milan, Stanković, Slaviša, Gavrilović, Veljko, Fira, Đorđe, "Molecular assessment of genetic diversity of Xanthomonas arboricola pv. juglandis strains from Serbia by various DNA fingerprinting techniques" in European Journal of Plant Pathology, 141, no. 1 (2015):133-145,
https://doi.org/10.1007/s10658-014-0531-5 . .

TY  - JOUR
AU  - Lozo, Jelena
AU  - Berić, Tanja
AU  - Terzić-Vidojević, Amarela
AU  - Stanković, Slaviša
AU  - Fira, Đorđe
AU  - Stanisavljević, L.
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/817
AB  - Using cultivation-dependant method, we isolated 184 strains from fresh and old bee bread, pollen, larvae and adults of solitary bee Osmia cornuta. The 16S rDNA sequencing of 79 selected isolates gave the final species-specific identification of strains. Phylogenetic analysis indicated that microbiota isolated from five different sources were represented with 29 species within three different phyla, Firmicutes with 25 species, Actinobacteria with only one species and Proteobacteria with three species of Enterobacteriaceae. Bacterial biodiversity presented with Shannon-Wiener index (H') was highest in the alimentary tract of adults and old bee bread (H' = 2.43 and H' = 2.53, respectively) and in the same time no dominance of any species was scored. On the contrary, results obtained for Simpson index (D) showed that in pollen samples the dominant species was Pantoea agglomerans (D = 0.42) while in fresh bee bread that was Staphylococcus sp. (D = 0.27). We assume that microbial diversity detected in the tested samples of solitary bee O. cornuta probably come from environment.
PB  - Cambridge Univ Press, Cambridge
T2  - Bulletin of Entomological Research
T1  - Microbiota associated with pollen, bee bread, larvae and adults of solitary bee Osmia cornuta (Hymenoptera: Megachilidae)
EP  - 476
IS  - 4
SP  - 470
VL  - 105
DO  - 10.1017/S0007485315000292
ER  - 

@article{
author = "Lozo, Jelena and Berić, Tanja and Terzić-Vidojević, Amarela and Stanković, Slaviša and Fira, Đorđe and Stanisavljević, L.",
year = "2015",
abstract = "Using cultivation-dependant method, we isolated 184 strains from fresh and old bee bread, pollen, larvae and adults of solitary bee Osmia cornuta. The 16S rDNA sequencing of 79 selected isolates gave the final species-specific identification of strains. Phylogenetic analysis indicated that microbiota isolated from five different sources were represented with 29 species within three different phyla, Firmicutes with 25 species, Actinobacteria with only one species and Proteobacteria with three species of Enterobacteriaceae. Bacterial biodiversity presented with Shannon-Wiener index (H') was highest in the alimentary tract of adults and old bee bread (H' = 2.43 and H' = 2.53, respectively) and in the same time no dominance of any species was scored. On the contrary, results obtained for Simpson index (D) showed that in pollen samples the dominant species was Pantoea agglomerans (D = 0.42) while in fresh bee bread that was Staphylococcus sp. (D = 0.27). We assume that microbial diversity detected in the tested samples of solitary bee O. cornuta probably come from environment.",
publisher = "Cambridge Univ Press, Cambridge",
journal = "Bulletin of Entomological Research",
title = "Microbiota associated with pollen, bee bread, larvae and adults of solitary bee Osmia cornuta (Hymenoptera: Megachilidae)",
pages = "476-470",
number = "4",
volume = "105",
doi = "10.1017/S0007485315000292"
}

Lozo, J., Berić, T., Terzić-Vidojević, A., Stanković, S., Fira, Đ.,& Stanisavljević, L.. (2015). Microbiota associated with pollen, bee bread, larvae and adults of solitary bee Osmia cornuta (Hymenoptera: Megachilidae). in Bulletin of Entomological Research
Cambridge Univ Press, Cambridge., 105(4), 470-476.
https://doi.org/10.1017/S0007485315000292

Lozo J, Berić T, Terzić-Vidojević A, Stanković S, Fira Đ, Stanisavljević L. Microbiota associated with pollen, bee bread, larvae and adults of solitary bee Osmia cornuta (Hymenoptera: Megachilidae). in Bulletin of Entomological Research. 2015;105(4):470-476.
doi:10.1017/S0007485315000292 .

Lozo, Jelena, Berić, Tanja, Terzić-Vidojević, Amarela, Stanković, Slaviša, Fira, Đorđe, Stanisavljević, L., "Microbiota associated with pollen, bee bread, larvae and adults of solitary bee Osmia cornuta (Hymenoptera: Megachilidae)" in Bulletin of Entomological Research, 105, no. 4 (2015):470-476,
https://doi.org/10.1017/S0007485315000292 . .

TY  - JOUR
AU  - Berić, Tanja
AU  - Stanković, Slaviša
AU  - Draganić, V.
AU  - Kojić, Milan
AU  - Lozo, Jelena
AU  - Fira, Đorđe
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/792
PB  - Wiley, Hoboken
T2  - Journal of Applied Microbiology
T1  - Novel antilisterial bacteriocin licheniocin 50.2 from Bacillus licheniformis VPS50.2 isolated from soil sample
EP  - 510
IS  - 3
SP  - 502
VL  - 116
DO  - 10.1111/jam.12393
ER  - 

@article{
author = "Berić, Tanja and Stanković, Slaviša and Draganić, V. and Kojić, Milan and Lozo, Jelena and Fira, Đorđe",
year = "2014",
publisher = "Wiley, Hoboken",
journal = "Journal of Applied Microbiology",
title = "Novel antilisterial bacteriocin licheniocin 50.2 from Bacillus licheniformis VPS50.2 isolated from soil sample",
pages = "510-502",
number = "3",
volume = "116",
doi = "10.1111/jam.12393"
}

Berić, T., Stanković, S., Draganić, V., Kojić, M., Lozo, J.,& Fira, Đ.. (2014). Novel antilisterial bacteriocin licheniocin 50.2 from Bacillus licheniformis VPS50.2 isolated from soil sample. in Journal of Applied Microbiology
Wiley, Hoboken., 116(3), 502-510.
https://doi.org/10.1111/jam.12393

Berić T, Stanković S, Draganić V, Kojić M, Lozo J, Fira Đ. Novel antilisterial bacteriocin licheniocin 50.2 from Bacillus licheniformis VPS50.2 isolated from soil sample. in Journal of Applied Microbiology. 2014;116(3):502-510.
doi:10.1111/jam.12393 .

Berić, Tanja, Stanković, Slaviša, Draganić, V., Kojić, Milan, Lozo, Jelena, Fira, Đorđe, "Novel antilisterial bacteriocin licheniocin 50.2 from Bacillus licheniformis VPS50.2 isolated from soil sample" in Journal of Applied Microbiology, 116, no. 3 (2014):502-510,
https://doi.org/10.1111/jam.12393 . .

TY  - JOUR
AU  - Ivanović, Zarko
AU  - Stanković, Slaviša
AU  - Zivković, Svetlana
AU  - Gavrilović, Veljko
AU  - Kojić, Milan
AU  - Fira, Đorđe
PY  - 2012
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/564
AB  - Infection of fruit trees by Pseudomonas syringae is a potentially serious problem that may limit the establishment and sustained productivity of pome and stone fruit orchards in Serbia. To estimate possible diversity of Pseudomonas syringae fruit trees strains, we collected a set of strains in several areas of Serbia. The samples were taken from infected orchards with raspberry, plum, cherry, sour cherry, peach, pear and apple trees. Genetic diversity of P. syringae strains isolated from fruit trees was determined by using SpeI macrorestriction analysis of genomic DNAs by pulsed-field gel electrophoresis (PFGE) and REP-PCR. Molecular analysis showed that most of isolates had unique profiles, with the exception of isolates from plum and cherry that displayed profiles identical to each other and similar to P. syringae pv. morsprunorum. The study presented here clearly demonstrates the discriminative power of molecular techniques in enabling a detailed analysis of the genetic variations between strains of P. syringae from different pome and stone fruit hosts in Serbia.
PB  - Springer, Dordrecht
T2  - European Journal of Plant Pathology
T1  - Molecular characterization of Pseudomonas syringae isolates from fruit trees and raspberry in Serbia
EP  - 203
IS  - 1
SP  - 191
VL  - 134
DO  - 10.1007/s10658-012-9978-4
ER  - 

@article{
author = "Ivanović, Zarko and Stanković, Slaviša and Zivković, Svetlana and Gavrilović, Veljko and Kojić, Milan and Fira, Đorđe",
year = "2012",
abstract = "Infection of fruit trees by Pseudomonas syringae is a potentially serious problem that may limit the establishment and sustained productivity of pome and stone fruit orchards in Serbia. To estimate possible diversity of Pseudomonas syringae fruit trees strains, we collected a set of strains in several areas of Serbia. The samples were taken from infected orchards with raspberry, plum, cherry, sour cherry, peach, pear and apple trees. Genetic diversity of P. syringae strains isolated from fruit trees was determined by using SpeI macrorestriction analysis of genomic DNAs by pulsed-field gel electrophoresis (PFGE) and REP-PCR. Molecular analysis showed that most of isolates had unique profiles, with the exception of isolates from plum and cherry that displayed profiles identical to each other and similar to P. syringae pv. morsprunorum. The study presented here clearly demonstrates the discriminative power of molecular techniques in enabling a detailed analysis of the genetic variations between strains of P. syringae from different pome and stone fruit hosts in Serbia.",
publisher = "Springer, Dordrecht",
journal = "European Journal of Plant Pathology",
title = "Molecular characterization of Pseudomonas syringae isolates from fruit trees and raspberry in Serbia",
pages = "203-191",
number = "1",
volume = "134",
doi = "10.1007/s10658-012-9978-4"
}

Ivanović, Z., Stanković, S., Zivković, S., Gavrilović, V., Kojić, M.,& Fira, Đ.. (2012). Molecular characterization of Pseudomonas syringae isolates from fruit trees and raspberry in Serbia. in European Journal of Plant Pathology
Springer, Dordrecht., 134(1), 191-203.
https://doi.org/10.1007/s10658-012-9978-4

Ivanović Z, Stanković S, Zivković S, Gavrilović V, Kojić M, Fira Đ. Molecular characterization of Pseudomonas syringae isolates from fruit trees and raspberry in Serbia. in European Journal of Plant Pathology. 2012;134(1):191-203.
doi:10.1007/s10658-012-9978-4 .

Ivanović, Zarko, Stanković, Slaviša, Zivković, Svetlana, Gavrilović, Veljko, Kojić, Milan, Fira, Đorđe, "Molecular characterization of Pseudomonas syringae isolates from fruit trees and raspberry in Serbia" in European Journal of Plant Pathology, 134, no. 1 (2012):191-203,
https://doi.org/10.1007/s10658-012-9978-4 . .

TY  - JOUR
AU  - Berić, Tanja
AU  - Kojić, Milan
AU  - Stanković, Slaviša
AU  - Topisirović, Ljubiša
AU  - Degrassi, Giuliano
AU  - Myers, Michael
AU  - Venturi, Vittorio
AU  - Fira, Đorđe
PY  - 2012
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/574
AB  - Screening of 203 Bacillus sp. natural isolates for antimicrobial activity against phytopathogenic bacteria showed that 127 tested strains inhibit at least one sensitive strain, which illustrates their potential use as biocontrol agents. Among them, 104 isolates showed significant antagonism against Xanthomonas oryzae pv. oryzae, and only one of these (VPS50.2) synthesizes bacteriocin. An additional screening tested whether 51 isolates contained genes involved in the biosynthesis of lipopeptides of the iturin and surfactin classes. Results show that 33 isolates harbour the operon for iturin biosynthesis, and six of them carry the sfp gene, responsible for the biosynthesis of surfactin. Lipopeptide purification from the supernatant of isolate SS12.9 (identified as B. subtilis or B. amyloliquefaciens) was performed using ethyl acetate extraction, ultrafiltration and reversed phase HPLC. Mass spectrometry analysis confirmed that isolate SS12.9 produces a substance of the iturin class with potential for biocontrol of X. oryzae pv. oryzae.
PB  - University of Zagreb
T2  - Food Technology and Biotechnology
T1  - Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria
EP  - 31
IS  - 1
SP  - 25
VL  - 50
UR  - https://hdl.handle.net/21.15107/rcub_imagine_574
ER  - 

@article{
author = "Berić, Tanja and Kojić, Milan and Stanković, Slaviša and Topisirović, Ljubiša and Degrassi, Giuliano and Myers, Michael and Venturi, Vittorio and Fira, Đorđe",
year = "2012",
abstract = "Screening of 203 Bacillus sp. natural isolates for antimicrobial activity against phytopathogenic bacteria showed that 127 tested strains inhibit at least one sensitive strain, which illustrates their potential use as biocontrol agents. Among them, 104 isolates showed significant antagonism against Xanthomonas oryzae pv. oryzae, and only one of these (VPS50.2) synthesizes bacteriocin. An additional screening tested whether 51 isolates contained genes involved in the biosynthesis of lipopeptides of the iturin and surfactin classes. Results show that 33 isolates harbour the operon for iturin biosynthesis, and six of them carry the sfp gene, responsible for the biosynthesis of surfactin. Lipopeptide purification from the supernatant of isolate SS12.9 (identified as B. subtilis or B. amyloliquefaciens) was performed using ethyl acetate extraction, ultrafiltration and reversed phase HPLC. Mass spectrometry analysis confirmed that isolate SS12.9 produces a substance of the iturin class with potential for biocontrol of X. oryzae pv. oryzae.",
publisher = "University of Zagreb",
journal = "Food Technology and Biotechnology",
title = "Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria",
pages = "31-25",
number = "1",
volume = "50",
url = "https://hdl.handle.net/21.15107/rcub_imagine_574"
}

Berić, T., Kojić, M., Stanković, S., Topisirović, L., Degrassi, G., Myers, M., Venturi, V.,& Fira, Đ.. (2012). Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria. in Food Technology and Biotechnology
University of Zagreb., 50(1), 25-31.
https://hdl.handle.net/21.15107/rcub_imagine_574

Berić T, Kojić M, Stanković S, Topisirović L, Degrassi G, Myers M, Venturi V, Fira Đ. Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria. in Food Technology and Biotechnology. 2012;50(1):25-31.
https://hdl.handle.net/21.15107/rcub_imagine_574 .

Berić, Tanja, Kojić, Milan, Stanković, Slaviša, Topisirović, Ljubiša, Degrassi, Giuliano, Myers, Michael, Venturi, Vittorio, Fira, Đorđe, "Antimicrobial Activity of Bacillus sp Natural Isolates and Their Potential Use in the Biocontrol of Phytopathogenic Bacteria" in Food Technology and Biotechnology, 50, no. 1 (2012):25-31,
https://hdl.handle.net/21.15107/rcub_imagine_574 .