TY  - JOUR
AU  - Filipić, Brankica
AU  - Novović, Katarina
AU  - Studholme, David J.
AU  - Malešević, Milka
AU  - Mirković, Nemanja
AU  - Kojić, Milan
AU  - Jovčić, Branko
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1306
AB  - Long-term overuse of antibiotics has driven the propagation and spreading of antibiotic resistance genes (ARGs) such as efflux pumps in the environment, which can be transferred to clinically relevant pathogens. This study explored the abundance and diversity of ARGs and mobile genetic elements within bacterial communities from sediments of three Western Balkans glacial lakes: Plav Lake (high impact of human population), Black Lake (medium impact of human population) and Donje Bare Lake (remote lake, minimal impact of human population) via shotgun metagenomics. Assembled metagenomic sequences revealed that Resistance-Nodulation-Division (RND) efflux pumps genes were most abundant in metagenome from the Plav Lake. The Integron Finder bioinformatics tool detected 38clusters ofattCsiteslackingintegron-integrases (CALIN) elements: 20 from Plav Lake, four from Black Lake and 14 from Donje Bare Lake. A complete integron sequence was recovered only from the assembled metagenome from Plav Lake. Plasmid contents within the metagenomes were similar, with proportions of contigs being plasmid-related: 1.73% for Plav Lake, 1.59% for Black Lake and 1.64% for Donje Bare Lake. The investigation showed that RNDs and mobile genetic elements content correlated with human population impact.
PB  - IWA Publishing, London
T2  - Journal of Water and Health
T1  - Shotgun metagenomics reveals differences in antibiotic resistance genes among bacterial communities in Western Balkans glacial lakes sediments
EP  - 397
IS  - 3
SP  - 383
VL  - 18
DO  - 10.2166/wh.2020.227
ER  - 

@article{
author = "Filipić, Brankica and Novović, Katarina and Studholme, David J. and Malešević, Milka and Mirković, Nemanja and Kojić, Milan and Jovčić, Branko",
year = "2020",
abstract = "Long-term overuse of antibiotics has driven the propagation and spreading of antibiotic resistance genes (ARGs) such as efflux pumps in the environment, which can be transferred to clinically relevant pathogens. This study explored the abundance and diversity of ARGs and mobile genetic elements within bacterial communities from sediments of three Western Balkans glacial lakes: Plav Lake (high impact of human population), Black Lake (medium impact of human population) and Donje Bare Lake (remote lake, minimal impact of human population) via shotgun metagenomics. Assembled metagenomic sequences revealed that Resistance-Nodulation-Division (RND) efflux pumps genes were most abundant in metagenome from the Plav Lake. The Integron Finder bioinformatics tool detected 38clusters ofattCsiteslackingintegron-integrases (CALIN) elements: 20 from Plav Lake, four from Black Lake and 14 from Donje Bare Lake. A complete integron sequence was recovered only from the assembled metagenome from Plav Lake. Plasmid contents within the metagenomes were similar, with proportions of contigs being plasmid-related: 1.73% for Plav Lake, 1.59% for Black Lake and 1.64% for Donje Bare Lake. The investigation showed that RNDs and mobile genetic elements content correlated with human population impact.",
publisher = "IWA Publishing, London",
journal = "Journal of Water and Health",
title = "Shotgun metagenomics reveals differences in antibiotic resistance genes among bacterial communities in Western Balkans glacial lakes sediments",
pages = "397-383",
number = "3",
volume = "18",
doi = "10.2166/wh.2020.227"
}

Filipić, B., Novović, K., Studholme, D. J., Malešević, M., Mirković, N., Kojić, M.,& Jovčić, B.. (2020). Shotgun metagenomics reveals differences in antibiotic resistance genes among bacterial communities in Western Balkans glacial lakes sediments. in Journal of Water and Health
IWA Publishing, London., 18(3), 383-397.
https://doi.org/10.2166/wh.2020.227

Filipić B, Novović K, Studholme DJ, Malešević M, Mirković N, Kojić M, Jovčić B. Shotgun metagenomics reveals differences in antibiotic resistance genes among bacterial communities in Western Balkans glacial lakes sediments. in Journal of Water and Health. 2020;18(3):383-397.
doi:10.2166/wh.2020.227 .

Filipić, Brankica, Novović, Katarina, Studholme, David J., Malešević, Milka, Mirković, Nemanja, Kojić, Milan, Jovčić, Branko, "Shotgun metagenomics reveals differences in antibiotic resistance genes among bacterial communities in Western Balkans glacial lakes sediments" in Journal of Water and Health, 18, no. 3 (2020):383-397,
https://doi.org/10.2166/wh.2020.227 . .

TY  - JOUR
AU  - Mirković, Nemanja
AU  - Kulas, Jelena
AU  - Miloradović, Zorana
AU  - Miljković, Marija
AU  - Tucović, Dina
AU  - Miocinović, Jelena
AU  - Jovčić, Branko
AU  - Mirkov, Ivana
AU  - Kojić, Milan
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1388
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 Miocinović, Jelena and Jovčić, 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., Miocinović, J., Jovčić, 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, Miocinović J, Jovčić 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, Miocinović, Jelena, Jovčić, 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  - 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  - Miljković, Marija
AU  - Jovanović, Sofija
AU  - O'Connor, Paula M.
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Filipić, Brankica
AU  - Dinić, Miroslav
AU  - Studholme, David John
AU  - Fira, Đorđe
AU  - Cotter, Paul D.
AU  - Kojić, Milan
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1264
AB  - Bacteria active against multi-drug resistant pathogens, isolated by direct selection of colonies from clover silage samples, produce zones of inhibition against two Gram-negative (Klebsiella pneumoniae Ni9 and Pseudomonas aeruginosa MMA83) and two Gram-positive (Staphylococcus aureus ATCC25923 and Listeria monocytogenes ATCC19111) pathogens. Isolates BGSP7, BGSP9, BGSP11 and BGSP12 produced the largest zones of inhibition against all four pathogens when grown in LB broth with aeration at 37 degrees C. Isolates BGSP7, BGSP9, BGSP11 and BGSP12 were identified as Brevibacillus laterosporus and pulsed field gel electrophoresis and extracellular protein profiles showed that three different strains (BGSP7, BGSP9 and BGSP11) were isolated. A semi-native SDS-PAGE (sodium dodecyl sulphate-polyacrylamide gel electrophoresis) gel overlay assay showed that BGSP7 and BGSP9 produce small antimicrobial molecules of about 1.5 kDa, while BGSP11 produces antimicrobial molecules of 1.5 and 6 kDa active against S. aureus ATCC25923. Amino acid analysis of two antimicrobial molecules (1583.73 Da; from BGSP7 and 1556.31 Da; from BGSP11) revealed that they have a similar composition and differ only by virtue of the presence of a methionine which is present only in BGSP11 molecule. Genome sequencing of the three isolates revealed the presence of gene clusters associated with the production of non-ribosomally synthesized peptides (brevibacillin, bogorol, gramicidin S, plipastatin and tyrocin) and bacteriocins (laterosporulin, a lactococcin 972-like bacteriocin, as well as putative linocin M18, sactipeptide, UviB and lantipeptide-like molecules). Ultimately, the purification of a number of antimicrobial molecules from each isolate suggests that they can be considered as potent biocontrol strains that produce an arsenal of antimicrobial molecules active against Gram-positive and Gram-negative multi-resistant pathogens, fungi and insects.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - Brevibacillus laterosporus strains BGSP7, BGSP9 and BGSP11 isolated from silage produce broad spectrum multi-antimicrobials
IS  - 5
VL  - 14
DO  - 10.1371/journal.pone.0216773
ER  - 

@article{
author = "Miljković, Marija and Jovanović, Sofija and O'Connor, Paula M. and Mirković, Nemanja and Jovčić, Branko and Filipić, Brankica and Dinić, Miroslav and Studholme, David John and Fira, Đorđe and Cotter, Paul D. and Kojić, Milan",
year = "2019",
abstract = "Bacteria active against multi-drug resistant pathogens, isolated by direct selection of colonies from clover silage samples, produce zones of inhibition against two Gram-negative (Klebsiella pneumoniae Ni9 and Pseudomonas aeruginosa MMA83) and two Gram-positive (Staphylococcus aureus ATCC25923 and Listeria monocytogenes ATCC19111) pathogens. Isolates BGSP7, BGSP9, BGSP11 and BGSP12 produced the largest zones of inhibition against all four pathogens when grown in LB broth with aeration at 37 degrees C. Isolates BGSP7, BGSP9, BGSP11 and BGSP12 were identified as Brevibacillus laterosporus and pulsed field gel electrophoresis and extracellular protein profiles showed that three different strains (BGSP7, BGSP9 and BGSP11) were isolated. A semi-native SDS-PAGE (sodium dodecyl sulphate-polyacrylamide gel electrophoresis) gel overlay assay showed that BGSP7 and BGSP9 produce small antimicrobial molecules of about 1.5 kDa, while BGSP11 produces antimicrobial molecules of 1.5 and 6 kDa active against S. aureus ATCC25923. Amino acid analysis of two antimicrobial molecules (1583.73 Da; from BGSP7 and 1556.31 Da; from BGSP11) revealed that they have a similar composition and differ only by virtue of the presence of a methionine which is present only in BGSP11 molecule. Genome sequencing of the three isolates revealed the presence of gene clusters associated with the production of non-ribosomally synthesized peptides (brevibacillin, bogorol, gramicidin S, plipastatin and tyrocin) and bacteriocins (laterosporulin, a lactococcin 972-like bacteriocin, as well as putative linocin M18, sactipeptide, UviB and lantipeptide-like molecules). Ultimately, the purification of a number of antimicrobial molecules from each isolate suggests that they can be considered as potent biocontrol strains that produce an arsenal of antimicrobial molecules active against Gram-positive and Gram-negative multi-resistant pathogens, fungi and insects.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "Brevibacillus laterosporus strains BGSP7, BGSP9 and BGSP11 isolated from silage produce broad spectrum multi-antimicrobials",
number = "5",
volume = "14",
doi = "10.1371/journal.pone.0216773"
}

Miljković, M., Jovanović, S., O'Connor, P. M., Mirković, N., Jovčić, B., Filipić, B., Dinić, M., Studholme, D. J., Fira, Đ., Cotter, P. D.,& Kojić, M.. (2019). Brevibacillus laterosporus strains BGSP7, BGSP9 and BGSP11 isolated from silage produce broad spectrum multi-antimicrobials. in PLoS One
Public Library Science, San Francisco., 14(5).
https://doi.org/10.1371/journal.pone.0216773

Miljković M, Jovanović S, O'Connor PM, Mirković N, Jovčić B, Filipić B, Dinić M, Studholme DJ, Fira Đ, Cotter PD, Kojić M. Brevibacillus laterosporus strains BGSP7, BGSP9 and BGSP11 isolated from silage produce broad spectrum multi-antimicrobials. in PLoS One. 2019;14(5).
doi:10.1371/journal.pone.0216773 .

Miljković, Marija, Jovanović, Sofija, O'Connor, Paula M., Mirković, Nemanja, Jovčić, Branko, Filipić, Brankica, Dinić, Miroslav, Studholme, David John, Fira, Đorđe, Cotter, Paul D., Kojić, Milan, "Brevibacillus laterosporus strains BGSP7, BGSP9 and BGSP11 isolated from silage produce broad spectrum multi-antimicrobials" in PLoS One, 14, no. 5 (2019),
https://doi.org/10.1371/journal.pone.0216773 . .

TY  - JOUR
AU  - Novović, Katarina
AU  - Malešević, Milka
AU  - Filipić, Brankica
AU  - Mirković, Nemanja L.
AU  - Miljković, Marija S.
AU  - Kojić, Milan
AU  - Jovčić, Branko
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1270
AB  - Pseudomonas aeruginosa, which is a clinically important representative of Pseudomonas spp., has been recognized as causative agent of severe nosocomial infections worldwide. An increase in antibiotic resistance of P. aeruginosa clinical strains could be attributed to their capacity to acquire resistance through mobile genetic elements such as mobile integrons that are present in one-half of multidrug-resistant P. aeruginosa strains. Mobile class 1 integrons are recognized as genetic elements involved in the rapid dissemination of multiple genes encoding for antibiotic resistance. The LexA protein is a major repressor of integrase transcription, but differences in transcription regulation among bacterial species have also been noted. In this study, the promoter activity of class 1 integron integrase gene (intI1) and its variant lacking the LexA binding site in Pseudomonas putida WCS358 wild type, rpoS and psrA was analysed. The results show that the activity of the intI1 gene promoter decreased in the rpoS and psrA mutants in the stationary phase of growth compared to the wild type, which indicates the role of RpoS and PsrA proteins in the positive regulation of integrase transcription. Additionally, it was determined that the activity of the lexA gene promoter decreased in rpoS and psrA, and thus, we propose that PsrA indirectly regulates the intI1 gene promoter activity through regulation of lexA gene expression in co-operation with some additional regulators. In this study, intI1 gene expression was shown to be controlled by two major stress response (SOS and RpoS) regulons, which indicates that integrase has evolved to use both systems to sense the cell status.
PB  - Springer, New York
T2  - Current Microbiology
T1  - PsrA Regulator Connects Cell Physiology and Class 1 Integron Integrase Gene Expression Through the Regulation of lexA Gene Expression in Pseudomonas spp.
EP  - 328
IS  - 3
SP  - 320
VL  - 76
DO  - 10.1007/s00284-019-01626-7
ER  - 

@article{
author = "Novović, Katarina and Malešević, Milka and Filipić, Brankica and Mirković, Nemanja L. and Miljković, Marija S. and Kojić, Milan and Jovčić, Branko",
year = "2019",
abstract = "Pseudomonas aeruginosa, which is a clinically important representative of Pseudomonas spp., has been recognized as causative agent of severe nosocomial infections worldwide. An increase in antibiotic resistance of P. aeruginosa clinical strains could be attributed to their capacity to acquire resistance through mobile genetic elements such as mobile integrons that are present in one-half of multidrug-resistant P. aeruginosa strains. Mobile class 1 integrons are recognized as genetic elements involved in the rapid dissemination of multiple genes encoding for antibiotic resistance. The LexA protein is a major repressor of integrase transcription, but differences in transcription regulation among bacterial species have also been noted. In this study, the promoter activity of class 1 integron integrase gene (intI1) and its variant lacking the LexA binding site in Pseudomonas putida WCS358 wild type, rpoS and psrA was analysed. The results show that the activity of the intI1 gene promoter decreased in the rpoS and psrA mutants in the stationary phase of growth compared to the wild type, which indicates the role of RpoS and PsrA proteins in the positive regulation of integrase transcription. Additionally, it was determined that the activity of the lexA gene promoter decreased in rpoS and psrA, and thus, we propose that PsrA indirectly regulates the intI1 gene promoter activity through regulation of lexA gene expression in co-operation with some additional regulators. In this study, intI1 gene expression was shown to be controlled by two major stress response (SOS and RpoS) regulons, which indicates that integrase has evolved to use both systems to sense the cell status.",
publisher = "Springer, New York",
journal = "Current Microbiology",
title = "PsrA Regulator Connects Cell Physiology and Class 1 Integron Integrase Gene Expression Through the Regulation of lexA Gene Expression in Pseudomonas spp.",
pages = "328-320",
number = "3",
volume = "76",
doi = "10.1007/s00284-019-01626-7"
}

Novović, K., Malešević, M., Filipić, B., Mirković, N. L., Miljković, M. S., Kojić, M.,& Jovčić, B.. (2019). PsrA Regulator Connects Cell Physiology and Class 1 Integron Integrase Gene Expression Through the Regulation of lexA Gene Expression in Pseudomonas spp.. in Current Microbiology
Springer, New York., 76(3), 320-328.
https://doi.org/10.1007/s00284-019-01626-7

Novović K, Malešević M, Filipić B, Mirković NL, Miljković MS, Kojić M, Jovčić B. PsrA Regulator Connects Cell Physiology and Class 1 Integron Integrase Gene Expression Through the Regulation of lexA Gene Expression in Pseudomonas spp.. in Current Microbiology. 2019;76(3):320-328.
doi:10.1007/s00284-019-01626-7 .

Novović, Katarina, Malešević, Milka, Filipić, Brankica, Mirković, Nemanja L., Miljković, Marija S., Kojić, Milan, Jovčić, Branko, "PsrA Regulator Connects Cell Physiology and Class 1 Integron Integrase Gene Expression Through the Regulation of lexA Gene Expression in Pseudomonas spp." in Current Microbiology, 76, no. 3 (2019):320-328,
https://doi.org/10.1007/s00284-019-01626-7 . .

TY  - JOUR
AU  - Malešević, Milka
AU  - Mirković, Nemanja
AU  - Lozo, Jelena
AU  - Novović, Katarina
AU  - Filipić, Brankica
AU  - Kojić, Milan
AU  - Jovčić, Branko
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1297
AB  - 16S rRNA gene-based metagenomic approach was used to assess the biodiversity of bacterial communities in the sediments of selected glacial lakes in the Western Balkans and to assess the impact of human population on these microbial communities. Sediment samples were collected from three glacial lakes, viz., Plav Lake (in a zone of the highest impact of human population), Black Lake (a zone of medium impact of human population), and Donje Bare Lake (a remote lake with minimal impact of human population). Canonical correlation analysis analysis indicated correlation between the distance of the lake from urbanized population and bacterial diversity in Donje Bare Lake sediment. Bacterial diversity of Black Lake sediment was correlated with high content of phosphorous and pH value. Chemical compounds exhibiting the most prominent correlation with bacterial diversity of Plav Lake were NH4-N, K2O, CaCo3, and total nitrogen . Additionally, CCA analysis indicated that population density was correlated with biodiversity of bacterial communities in Plav Lake sediment, which is the most exposed to human population. Multivariate regression revealed the highest correlation between the presence of Proteobacteria classes and population density and levels of NH4-N. The influence of human population was observed to be important for shaping the sediment communities in addition to biological and chemical factors.
PB  - Taylor & Francis Inc, Philadelphia
T2  - Geomicrobiology Journal
T1  - Bacterial Diversity among the Sediments of Glacial Lakes in the Western Balkans: Exploring the Impact of Human Population
EP  - 270
IS  - 3
SP  - 261
VL  - 36
DO  - 10.1080/01490451.2018.1550128
ER  - 

@article{
author = "Malešević, Milka and Mirković, Nemanja and Lozo, Jelena and Novović, Katarina and Filipić, Brankica and Kojić, Milan and Jovčić, Branko",
year = "2019",
abstract = "16S rRNA gene-based metagenomic approach was used to assess the biodiversity of bacterial communities in the sediments of selected glacial lakes in the Western Balkans and to assess the impact of human population on these microbial communities. Sediment samples were collected from three glacial lakes, viz., Plav Lake (in a zone of the highest impact of human population), Black Lake (a zone of medium impact of human population), and Donje Bare Lake (a remote lake with minimal impact of human population). Canonical correlation analysis analysis indicated correlation between the distance of the lake from urbanized population and bacterial diversity in Donje Bare Lake sediment. Bacterial diversity of Black Lake sediment was correlated with high content of phosphorous and pH value. Chemical compounds exhibiting the most prominent correlation with bacterial diversity of Plav Lake were NH4-N, K2O, CaCo3, and total nitrogen . Additionally, CCA analysis indicated that population density was correlated with biodiversity of bacterial communities in Plav Lake sediment, which is the most exposed to human population. Multivariate regression revealed the highest correlation between the presence of Proteobacteria classes and population density and levels of NH4-N. The influence of human population was observed to be important for shaping the sediment communities in addition to biological and chemical factors.",
publisher = "Taylor & Francis Inc, Philadelphia",
journal = "Geomicrobiology Journal",
title = "Bacterial Diversity among the Sediments of Glacial Lakes in the Western Balkans: Exploring the Impact of Human Population",
pages = "270-261",
number = "3",
volume = "36",
doi = "10.1080/01490451.2018.1550128"
}

Malešević, M., Mirković, N., Lozo, J., Novović, K., Filipić, B., Kojić, M.,& Jovčić, B.. (2019). Bacterial Diversity among the Sediments of Glacial Lakes in the Western Balkans: Exploring the Impact of Human Population. in Geomicrobiology Journal
Taylor & Francis Inc, Philadelphia., 36(3), 261-270.
https://doi.org/10.1080/01490451.2018.1550128

Malešević M, Mirković N, Lozo J, Novović K, Filipić B, Kojić M, Jovčić B. Bacterial Diversity among the Sediments of Glacial Lakes in the Western Balkans: Exploring the Impact of Human Population. in Geomicrobiology Journal. 2019;36(3):261-270.
doi:10.1080/01490451.2018.1550128 .

Malešević, Milka, Mirković, Nemanja, Lozo, Jelena, Novović, Katarina, Filipić, Brankica, Kojić, Milan, Jovčić, Branko, "Bacterial Diversity among the Sediments of Glacial Lakes in the Western Balkans: Exploring the Impact of Human Population" in Geomicrobiology Journal, 36, no. 3 (2019):261-270,
https://doi.org/10.1080/01490451.2018.1550128 . .

TY  - JOUR
AU  - Miljković, Manja
AU  - Lozo, Jelena
AU  - Mirković, Nemanja
AU  - O'Connor, Paula M.
AU  - Malešević, Milka
AU  - Jovčić, Branko
AU  - Cotter, Paul D.
AU  - Kojić, Milan
PY  - 2018
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1124
AB  - The gene cluster responsible for the production of the aureocin A53-like bacteriocin, lactolisterin BU, is located on plasmid pBU6 in Lactococcus lactis subsp. lactis BGBU1-4. Heterologous expression of pBU6 confirmed that production and limited immunity to lactolisterin BU were provided by the plasmid. Comparative analysis of aureocin A53-like operons revealed that the structural genes shared a low level of identity, while other genes were without homology, indicating a different origin. Subcloning and expression of genes located downstream of the structural gene, IliBU, revealed that the lactolisterin BU cluster consists of four genes: the structural gene IliBU, the abcT gene encoding an ABC transporter, the accL gene encoding an accessory protein and the immL gene which provides limited immunity to lactolisterin BU. Reverse transcription analysis revealed that all genes were transcribed as one polycistronic mRNA. Attempts to split the lactolisterin BU operon, even when both parts were under control of the PlliBU promoter, were unsuccessful indicating that expression of lactolisterin BU is probably precisely regulated at the translational level by translational coupling and is possible only when all genes of the operon are in cis constellation. Two rho-independent transcription terminators were detected in the lactolisterin BU operon: the first in the intergenic region of the IliBU and abcT genes and the second at the end of operon. Deletion of the second transcription terminator did not influence production of the bacteriocin in lactococci.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - Functional Characterization of the Lactolisterin BU Gene Cluster of Lactococcus lactis subsp. lactis BGBU1-4
VL  - 9
DO  - 10.3389/fmicb.2018.02774
ER  - 

@article{
author = "Miljković, Manja and Lozo, Jelena and Mirković, Nemanja and O'Connor, Paula M. and Malešević, Milka and Jovčić, Branko and Cotter, Paul D. and Kojić, Milan",
year = "2018",
abstract = "The gene cluster responsible for the production of the aureocin A53-like bacteriocin, lactolisterin BU, is located on plasmid pBU6 in Lactococcus lactis subsp. lactis BGBU1-4. Heterologous expression of pBU6 confirmed that production and limited immunity to lactolisterin BU were provided by the plasmid. Comparative analysis of aureocin A53-like operons revealed that the structural genes shared a low level of identity, while other genes were without homology, indicating a different origin. Subcloning and expression of genes located downstream of the structural gene, IliBU, revealed that the lactolisterin BU cluster consists of four genes: the structural gene IliBU, the abcT gene encoding an ABC transporter, the accL gene encoding an accessory protein and the immL gene which provides limited immunity to lactolisterin BU. Reverse transcription analysis revealed that all genes were transcribed as one polycistronic mRNA. Attempts to split the lactolisterin BU operon, even when both parts were under control of the PlliBU promoter, were unsuccessful indicating that expression of lactolisterin BU is probably precisely regulated at the translational level by translational coupling and is possible only when all genes of the operon are in cis constellation. Two rho-independent transcription terminators were detected in the lactolisterin BU operon: the first in the intergenic region of the IliBU and abcT genes and the second at the end of operon. Deletion of the second transcription terminator did not influence production of the bacteriocin in lactococci.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "Functional Characterization of the Lactolisterin BU Gene Cluster of Lactococcus lactis subsp. lactis BGBU1-4",
volume = "9",
doi = "10.3389/fmicb.2018.02774"
}

Miljković, M., Lozo, J., Mirković, N., O'Connor, P. M., Malešević, M., Jovčić, B., Cotter, P. D.,& Kojić, M.. (2018). Functional Characterization of the Lactolisterin BU Gene Cluster of Lactococcus lactis subsp. lactis BGBU1-4. in Frontiers in Microbiology
Frontiers Media Sa, Lausanne., 9.
https://doi.org/10.3389/fmicb.2018.02774

Miljković M, Lozo J, Mirković N, O'Connor PM, Malešević M, Jovčić B, Cotter PD, Kojić M. Functional Characterization of the Lactolisterin BU Gene Cluster of Lactococcus lactis subsp. lactis BGBU1-4. in Frontiers in Microbiology. 2018;9.
doi:10.3389/fmicb.2018.02774 .

Miljković, Manja, Lozo, Jelena, Mirković, Nemanja, O'Connor, Paula M., Malešević, Milka, Jovčić, Branko, Cotter, Paul D., Kojić, Milan, "Functional Characterization of the Lactolisterin BU Gene Cluster of Lactococcus lactis subsp. lactis BGBU1-4" in Frontiers in Microbiology, 9 (2018),
https://doi.org/10.3389/fmicb.2018.02774 . .

TY  - JOUR
AU  - Lozo, Jelena
AU  - Mirković, Nemanja
AU  - O'Connor, Paula M.
AU  - Malešević, Milka
AU  - Miljković, Marija
AU  - Polović, Natalija
AU  - Jovčić, Branko
AU  - Cotter, Paul D.
AU  - Kojić, Milan
PY  - 2017
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1001
AB  - Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4
IS  - 21
VL  - 83
DO  - 10.1128/AEM.01519-17
ER  - 

@article{
author = "Lozo, Jelena and Mirković, Nemanja and O'Connor, Paula M. and Malešević, Milka and Miljković, Marija and Polović, Natalija and Jovčić, Branko and Cotter, Paul D. and Kojić, Milan",
year = "2017",
abstract = "Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4",
number = "21",
volume = "83",
doi = "10.1128/AEM.01519-17"
}

Lozo, J., Mirković, N., O'Connor, P. M., Malešević, M., Miljković, M., Polović, N., Jovčić, B., Cotter, P. D.,& Kojić, M.. (2017). Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 83(21).
https://doi.org/10.1128/AEM.01519-17

Lozo J, Mirković N, O'Connor PM, Malešević M, Miljković M, Polović N, Jovčić B, Cotter PD, Kojić M. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology. 2017;83(21).
doi:10.1128/AEM.01519-17 .

Lozo, Jelena, Mirković, Nemanja, O'Connor, Paula M., Malešević, Milka, Miljković, Marija, Polović, Natalija, Jovčić, Branko, Cotter, Paul D., Kojić, Milan, "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4" in Applied and Environmental Microbiology, 83, no. 21 (2017),
https://doi.org/10.1128/AEM.01519-17 . .

TY  - JOUR
AU  - Lukić, Jovanka
AU  - Jancić, I.
AU  - Mirković, N.
AU  - Bufan, B.
AU  - Đokić, Jelena
AU  - Milenković, M.
AU  - Begović, Jelena
AU  - Strahinić, Ivana
AU  - Lozo, Jelena
PY  - 2017
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1003
AB  - In the light of the increasing resistance of bacterial pathogens to antibiotics, one of the main global strategies in applied science is development of alternative treatments, which would be safe both for the host and from the environmental perspective. Accordingly, the aim of this study was to test whether two lactic acid bacteria (LAB) strains, Lactococcus lactis BGBU1-4 and Lactobacillus salivarius BGHO1, could be applied as safe supplements for Listeria infection. Two major research objectives were set: to compare the effects of BGBU1-4 and BGHO1 on early immune response in gut tissue of Wistar rats co-administered with Listeria monocytogenes ATCC19111 and next, to test how this applies to their usage as therapeutics in acute ATCC19111 infection. Intestinal villi (IV), Peyer's patches (PP) and mesenteric lymph nodes (MLN) were used for the analysis. The results showed that BGHO1 increased the mRNA expression of innate immune markers CD14, interleukin (IL)-1 beta and tumour necrosis factor (TNF)-alpha in PP and IV, and, in parallel, caused a decrease of listeriolysin O (LLO) mRNA expression in same tissues. In MLN of BGHO1 treated rats, LLO expression was increased, along with an increase of the expression of OX-62 mRNA and CD69, pointing to the activation of adaptive immunity. On the other hand, in BGBU1-4 treated rats, there was no reduction of LLO mRNA expression and no induction of innate immunity markers in intestinal tissue. Additionally, CD14 and IL-1 beta, as well as LLO, but not OX-62 mRNA and CD69 expression, were elevated in MLN of BGBU1-4 treated rats. However, when applied therapeutically, both, BGBU1-4 and BGHO1, lowered Listeria count in spleens of infected rats. Our results not only reveal the potential of LAB to ameliorate Listeria infections, but suggest different immunological effects of two different LAB strains, both of which could be effective in Listeria elimination.
PB  - Wageningen Academic Publishers, Wageningen
T2  - Beneficial Microbes
T1  - Lactococcus lactis and Lactobacillus salivarius differently modulate early immunological response of Wistar rats co-administered with Listeria monocytogenes
EP  - 822
IS  - 5
SP  - 809
VL  - 8
DO  - 10.3920/BM2017.0007
ER  - 

@article{
author = "Lukić, Jovanka and Jancić, I. and Mirković, N. and Bufan, B. and Đokić, Jelena and Milenković, M. and Begović, Jelena and Strahinić, Ivana and Lozo, Jelena",
year = "2017",
abstract = "In the light of the increasing resistance of bacterial pathogens to antibiotics, one of the main global strategies in applied science is development of alternative treatments, which would be safe both for the host and from the environmental perspective. Accordingly, the aim of this study was to test whether two lactic acid bacteria (LAB) strains, Lactococcus lactis BGBU1-4 and Lactobacillus salivarius BGHO1, could be applied as safe supplements for Listeria infection. Two major research objectives were set: to compare the effects of BGBU1-4 and BGHO1 on early immune response in gut tissue of Wistar rats co-administered with Listeria monocytogenes ATCC19111 and next, to test how this applies to their usage as therapeutics in acute ATCC19111 infection. Intestinal villi (IV), Peyer's patches (PP) and mesenteric lymph nodes (MLN) were used for the analysis. The results showed that BGHO1 increased the mRNA expression of innate immune markers CD14, interleukin (IL)-1 beta and tumour necrosis factor (TNF)-alpha in PP and IV, and, in parallel, caused a decrease of listeriolysin O (LLO) mRNA expression in same tissues. In MLN of BGHO1 treated rats, LLO expression was increased, along with an increase of the expression of OX-62 mRNA and CD69, pointing to the activation of adaptive immunity. On the other hand, in BGBU1-4 treated rats, there was no reduction of LLO mRNA expression and no induction of innate immunity markers in intestinal tissue. Additionally, CD14 and IL-1 beta, as well as LLO, but not OX-62 mRNA and CD69 expression, were elevated in MLN of BGBU1-4 treated rats. However, when applied therapeutically, both, BGBU1-4 and BGHO1, lowered Listeria count in spleens of infected rats. Our results not only reveal the potential of LAB to ameliorate Listeria infections, but suggest different immunological effects of two different LAB strains, both of which could be effective in Listeria elimination.",
publisher = "Wageningen Academic Publishers, Wageningen",
journal = "Beneficial Microbes",
title = "Lactococcus lactis and Lactobacillus salivarius differently modulate early immunological response of Wistar rats co-administered with Listeria monocytogenes",
pages = "822-809",
number = "5",
volume = "8",
doi = "10.3920/BM2017.0007"
}

Lukić, J., Jancić, I., Mirković, N., Bufan, B., Đokić, J., Milenković, M., Begović, J., Strahinić, I.,& Lozo, J.. (2017). Lactococcus lactis and Lactobacillus salivarius differently modulate early immunological response of Wistar rats co-administered with Listeria monocytogenes. in Beneficial Microbes
Wageningen Academic Publishers, Wageningen., 8(5), 809-822.
https://doi.org/10.3920/BM2017.0007

Lukić J, Jancić I, Mirković N, Bufan B, Đokić J, Milenković M, Begović J, Strahinić I, Lozo J. Lactococcus lactis and Lactobacillus salivarius differently modulate early immunological response of Wistar rats co-administered with Listeria monocytogenes. in Beneficial Microbes. 2017;8(5):809-822.
doi:10.3920/BM2017.0007 .

Lukić, Jovanka, Jancić, I., Mirković, N., Bufan, B., Đokić, Jelena, Milenković, M., Begović, Jelena, Strahinić, Ivana, Lozo, Jelena, "Lactococcus lactis and Lactobacillus salivarius differently modulate early immunological response of Wistar rats co-administered with Listeria monocytogenes" in Beneficial Microbes, 8, no. 5 (2017):809-822,
https://doi.org/10.3920/BM2017.0007 . .

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 . .

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  - https://imagine.imgge.bg.ac.rs/handle/123456789/904
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  - 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 . .

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  - Novović, Katarina
AU  - Filipić, B.
AU  - Veljović, Katarina
AU  - Begović, Jelena
AU  - Mirković, N.
AU  - Jovčić, Branko
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/893
AB  - New Delhi metallo-beta-lactamase-1 (NDM-1) will soon become the most commonly isolated and distributed metallo-beta-lactamase worldwide due to its rapid international dissemination and its ability to be expressed by numerous Gram-negative pathogens. NDM-positive bacteria pose a significant public health threat in the Indian subcontinent and the Balkans, which have been designated as endemic regions. Our study was focused on urban rivers, a lake and springheads as a potential source of NDM-1-producing strains in Serbia, but also as a source of other metallo-beta-lactamases and extended-spectrum beta-lactamase (ESBL) producing bacteria. A total of 69 beta-lactam resistant isolates, belonging to 12 bacterial genera, were collected from 8 out of 10 different locations in Belgrade, of which the most were from a popular recreational site, Ada Ciganlija Lake. Phenotypic tests revealed 7 (10.14%) ESBL-producing isolates and 39 (56.52%) isolates resistant to imipenem, of which 32 were positive for metallo-beta-lactamase (MBL) production. PCR and sequencing revealed the presence of genetic determinants for SHV (3 isolates), DHA-1 (1 isolate) and CMY-2 (1 isolate) beta-lactamases. However, we did not detect any NDM-1-producing strains (previously described cases of NDM-1 from Serbia were limited to Belgrade), so we propose that Serbian NDM-1 is in fact a transplant and a nosocomial, rather than an environmental, issue and that Serbia is not an endemic region for NDM-1.
PB  - Elsevier, Amsterdam
T2  - Science of the Total Environment
T1  - Environmental waters and bla(NDm-1) in Belgrade, Serbia: Endemicity questioned
EP  - 398
SP  - 393
VL  - 511
DO  - 10.1016/j.scitotenv.2014.12.072
ER  - 

@article{
author = "Novović, Katarina and Filipić, B. and Veljović, Katarina and Begović, Jelena and Mirković, N. and Jovčić, Branko",
year = "2015",
abstract = "New Delhi metallo-beta-lactamase-1 (NDM-1) will soon become the most commonly isolated and distributed metallo-beta-lactamase worldwide due to its rapid international dissemination and its ability to be expressed by numerous Gram-negative pathogens. NDM-positive bacteria pose a significant public health threat in the Indian subcontinent and the Balkans, which have been designated as endemic regions. Our study was focused on urban rivers, a lake and springheads as a potential source of NDM-1-producing strains in Serbia, but also as a source of other metallo-beta-lactamases and extended-spectrum beta-lactamase (ESBL) producing bacteria. A total of 69 beta-lactam resistant isolates, belonging to 12 bacterial genera, were collected from 8 out of 10 different locations in Belgrade, of which the most were from a popular recreational site, Ada Ciganlija Lake. Phenotypic tests revealed 7 (10.14%) ESBL-producing isolates and 39 (56.52%) isolates resistant to imipenem, of which 32 were positive for metallo-beta-lactamase (MBL) production. PCR and sequencing revealed the presence of genetic determinants for SHV (3 isolates), DHA-1 (1 isolate) and CMY-2 (1 isolate) beta-lactamases. However, we did not detect any NDM-1-producing strains (previously described cases of NDM-1 from Serbia were limited to Belgrade), so we propose that Serbian NDM-1 is in fact a transplant and a nosocomial, rather than an environmental, issue and that Serbia is not an endemic region for NDM-1.",
publisher = "Elsevier, Amsterdam",
journal = "Science of the Total Environment",
title = "Environmental waters and bla(NDm-1) in Belgrade, Serbia: Endemicity questioned",
pages = "398-393",
volume = "511",
doi = "10.1016/j.scitotenv.2014.12.072"
}

Novović, K., Filipić, B., Veljović, K., Begović, J., Mirković, N.,& Jovčić, B.. (2015). Environmental waters and bla(NDm-1) in Belgrade, Serbia: Endemicity questioned. in Science of the Total Environment
Elsevier, Amsterdam., 511, 393-398.
https://doi.org/10.1016/j.scitotenv.2014.12.072

Novović K, Filipić B, Veljović K, Begović J, Mirković N, Jovčić B. Environmental waters and bla(NDm-1) in Belgrade, Serbia: Endemicity questioned. in Science of the Total Environment. 2015;511:393-398.
doi:10.1016/j.scitotenv.2014.12.072 .

Novović, Katarina, Filipić, B., Veljović, Katarina, Begović, Jelena, Mirković, N., Jovčić, Branko, "Environmental waters and bla(NDm-1) in Belgrade, Serbia: Endemicity questioned" in Science of the Total Environment, 511 (2015):393-398,
https://doi.org/10.1016/j.scitotenv.2014.12.072 . .