TY  - JOUR
AU  - Malešević, Milka
AU  - Stanisavljević, Nemanja
AU  - Novović, Katarina
AU  - Polović, Natalija
AU  - Vasiljević, Zorica
AU  - Kojić, Milan
AU  - Jovčić, Branko
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1338
AB  - Burkholderia cepacia is well known as the causative agent of infections in humans where often shares niche with other pathogens, like Pseudomonas aeruginosa. Clinical isolate Burkholderia sp. BCC4135 was selected due to its strong quorum quenching (QQ) activity. Whole genome sequencing unveiled this isolate as B. cepacia with unique sequence type ST1485 and a myriad of genes belonging to resistome and virulome. Two QQ lactonases YtnP and Y2-aiiA originated from B. cepacia BCC4135 were cloned, expressed, and functionally characterized. They were active against a broad substrate spectrum of the N-acyl-homoserine lactones (AHLs). The YtnP lactonase was inactive, while Y2-aiiA was active against N-tetradecanoyl-DL-homoserine lactone (C14-HSL) which could imply the difference in their biological roles from the aspect of its quorum sensing (QS) autoregulation and interference with the QS systems of bacteria residing within the same niche. Both YtnP and Y2-aiiA were able to attenuate virulence potential of P. aeruginosa MMA83 clinical isolate declining its biofilm formation and virulence factors production. B. cepacia BCC4135 lactonases interfered with the las, rhl, and even pqs QS circuit of P. aeruginosa MMA83 transcription and the effect of combined enzymes was even more prominent. B. cepacia BCC4135 also employs the CepI/R QS system for governing its own virulence traits and possibly self-regulates the QQ/QS network through the different expression and activity of YtnP and/or Y2-aiiA. Our findings pointed out that BCC4135 lactonases could be exploited as an effective antivirulence drugs against P. aeruginosa and gave us a new insight into B. cepacia QQ/QS machinery.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Microbial Pathogenesis
T1  - Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity
VL  - 149
DO  - 10.1016/j.micpath.2020.104561
ER  - 

@article{
author = "Malešević, Milka and Stanisavljević, Nemanja and Novović, Katarina and Polović, Natalija and Vasiljević, Zorica and Kojić, Milan and Jovčić, Branko",
year = "2020",
abstract = "Burkholderia cepacia is well known as the causative agent of infections in humans where often shares niche with other pathogens, like Pseudomonas aeruginosa. Clinical isolate Burkholderia sp. BCC4135 was selected due to its strong quorum quenching (QQ) activity. Whole genome sequencing unveiled this isolate as B. cepacia with unique sequence type ST1485 and a myriad of genes belonging to resistome and virulome. Two QQ lactonases YtnP and Y2-aiiA originated from B. cepacia BCC4135 were cloned, expressed, and functionally characterized. They were active against a broad substrate spectrum of the N-acyl-homoserine lactones (AHLs). The YtnP lactonase was inactive, while Y2-aiiA was active against N-tetradecanoyl-DL-homoserine lactone (C14-HSL) which could imply the difference in their biological roles from the aspect of its quorum sensing (QS) autoregulation and interference with the QS systems of bacteria residing within the same niche. Both YtnP and Y2-aiiA were able to attenuate virulence potential of P. aeruginosa MMA83 clinical isolate declining its biofilm formation and virulence factors production. B. cepacia BCC4135 lactonases interfered with the las, rhl, and even pqs QS circuit of P. aeruginosa MMA83 transcription and the effect of combined enzymes was even more prominent. B. cepacia BCC4135 also employs the CepI/R QS system for governing its own virulence traits and possibly self-regulates the QQ/QS network through the different expression and activity of YtnP and/or Y2-aiiA. Our findings pointed out that BCC4135 lactonases could be exploited as an effective antivirulence drugs against P. aeruginosa and gave us a new insight into B. cepacia QQ/QS machinery.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Microbial Pathogenesis",
title = "Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity",
volume = "149",
doi = "10.1016/j.micpath.2020.104561"
}

Malešević, M., Stanisavljević, N., Novović, K., Polović, N., Vasiljević, Z., Kojić, M.,& Jovčić, B.. (2020). Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity. in Microbial Pathogenesis
Academic Press Ltd- Elsevier Science Ltd, London., 149.
https://doi.org/10.1016/j.micpath.2020.104561

Malešević M, Stanisavljević N, Novović K, Polović N, Vasiljević Z, Kojić M, Jovčić B. Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity. in Microbial Pathogenesis. 2020;149.
doi:10.1016/j.micpath.2020.104561 .

Malešević, Milka, Stanisavljević, Nemanja, Novović, Katarina, Polović, Natalija, Vasiljević, Zorica, Kojić, Milan, Jovčić, Branko, "Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity" in Microbial Pathogenesis, 149 (2020),
https://doi.org/10.1016/j.micpath.2020.104561 . .

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  - Malešević, Milka
AU  - Di Lorenzo, Flaviana
AU  - Filipić, Brankica
AU  - Stanisavljević, Nemanja
AU  - Novović, Katarina
AU  - Šenerović, Lidija
AU  - Polović, Natalija
AU  - Molinaro, Antonio
AU  - Kojić, Milan
AU  - Jovčić, Branko
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1217
AB  - Pseudomonas aeruginosa is one of the most common opportunistic pathogens that use quorum sensing (QS) system to regulate virulence factors expression and biofilm development. Delftia sp. 11304 was selected among 663 Gram-negative clinical isolates based on its QS inhibitory activity against P. aeruginosa MMA83 clinical isolate. Whole genome sequencing identified this isolate as D. tsuruhatensis and revealed genetic armamentarium of virulence factors and antibiotic resistance determinants. Ethyl acetate extract of D. tsuruhatensis 11304 culture supernatant (QSI extract) prevented biofilm formation of P. aeruginosa MMA83, but was unable to cause biofilm decomposition. QSI extract showed a synergistic effect in combination with meropenem and gentamycin, against P. aeruginosa MMA83. A dose-dependent reduction of the virulence factors: elastase, rhamnolipid and pyocyanin production by P. aeruginosa MMA83 and significant downregulation of lasI, lasR, rhlI, rhlR, pqs and mvfR expression were observed. Matrix-assisted Laser Desorption Ionization (MALDI) mass spectrometry of D. tsuruhatensis 11304 QSI extract revealed the presence of N-acyl homoserine lactones (AHL) with chain lengths of C12 to C18. The main ion peak was identified as N-octadecanoylhomoserine lactone (C-18-HSL). Commercial C-18-HSL (20 mu M) reduced pyocyanin production as well as mRNA level of the lasI gene. A novel AHL species, dihydroxy-N-octadecanoylhomoserine lactone, was also described.
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Pseudomonas aeruginosa quorum sensing inhibition by clinical isolate Delftia tsuruhatensis 11304: involvement of N-octadecanoylhomoserine lactones
VL  - 9
DO  - 10.1038/s41598-019-52955-3
ER  - 

@article{
author = "Malešević, Milka and Di Lorenzo, Flaviana and Filipić, Brankica and Stanisavljević, Nemanja and Novović, Katarina and Šenerović, Lidija and Polović, Natalija and Molinaro, Antonio and Kojić, Milan and Jovčić, Branko",
year = "2019",
abstract = "Pseudomonas aeruginosa is one of the most common opportunistic pathogens that use quorum sensing (QS) system to regulate virulence factors expression and biofilm development. Delftia sp. 11304 was selected among 663 Gram-negative clinical isolates based on its QS inhibitory activity against P. aeruginosa MMA83 clinical isolate. Whole genome sequencing identified this isolate as D. tsuruhatensis and revealed genetic armamentarium of virulence factors and antibiotic resistance determinants. Ethyl acetate extract of D. tsuruhatensis 11304 culture supernatant (QSI extract) prevented biofilm formation of P. aeruginosa MMA83, but was unable to cause biofilm decomposition. QSI extract showed a synergistic effect in combination with meropenem and gentamycin, against P. aeruginosa MMA83. A dose-dependent reduction of the virulence factors: elastase, rhamnolipid and pyocyanin production by P. aeruginosa MMA83 and significant downregulation of lasI, lasR, rhlI, rhlR, pqs and mvfR expression were observed. Matrix-assisted Laser Desorption Ionization (MALDI) mass spectrometry of D. tsuruhatensis 11304 QSI extract revealed the presence of N-acyl homoserine lactones (AHL) with chain lengths of C12 to C18. The main ion peak was identified as N-octadecanoylhomoserine lactone (C-18-HSL). Commercial C-18-HSL (20 mu M) reduced pyocyanin production as well as mRNA level of the lasI gene. A novel AHL species, dihydroxy-N-octadecanoylhomoserine lactone, was also described.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Pseudomonas aeruginosa quorum sensing inhibition by clinical isolate Delftia tsuruhatensis 11304: involvement of N-octadecanoylhomoserine lactones",
volume = "9",
doi = "10.1038/s41598-019-52955-3"
}

Malešević, M., Di Lorenzo, F., Filipić, B., Stanisavljević, N., Novović, K., Šenerović, L., Polović, N., Molinaro, A., Kojić, M.,& Jovčić, B.. (2019). Pseudomonas aeruginosa quorum sensing inhibition by clinical isolate Delftia tsuruhatensis 11304: involvement of N-octadecanoylhomoserine lactones. in Scientific Reports
Nature Publishing Group, London., 9.
https://doi.org/10.1038/s41598-019-52955-3

Malešević M, Di Lorenzo F, Filipić B, Stanisavljević N, Novović K, Šenerović L, Polović N, Molinaro A, Kojić M, Jovčić B. Pseudomonas aeruginosa quorum sensing inhibition by clinical isolate Delftia tsuruhatensis 11304: involvement of N-octadecanoylhomoserine lactones. in Scientific Reports. 2019;9.
doi:10.1038/s41598-019-52955-3 .

Malešević, Milka, Di Lorenzo, Flaviana, Filipić, Brankica, Stanisavljević, Nemanja, Novović, Katarina, Šenerović, Lidija, Polović, Natalija, Molinaro, Antonio, Kojić, Milan, Jovčić, Branko, "Pseudomonas aeruginosa quorum sensing inhibition by clinical isolate Delftia tsuruhatensis 11304: involvement of N-octadecanoylhomoserine lactones" in Scientific Reports, 9 (2019),
https://doi.org/10.1038/s41598-019-52955-3 . .

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  - Rasković, Brankica
AU  - Lazić, Jelena
AU  - Polović, Natalija
PY  - 2016
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/972
AB  - BACKGROUNDThe physiological role of fig latex is to protect the plant from pathogens. Latex is a rich source of proteases, predominantly ficin. Fig latex also contains collagenolytic protease and chitinolytic enzymes. Our aim was to investigate changes in protein composition, enzyme and antifungal activities of fig latex during fruit ripening. RESULTSComparison of latex samples in different time periods showed a uniform increase of protein concentration in chronological order. The content of collagenolytic protease did not differ significantly in the latex samples, while the content of ficin decreased. Ficin-specific activity towards casein was the highest at the beginning of fruit development (about 80 U mg(-1)). Specific milk clotting activity increased as well as the abundance of casein band in the clots. Specific chitinolytic activity at the beginning of flowering was 6.5 times higher than the activity in the period when fruits are ripe. Antifungal activity is the most extensive in spring. CONCLUSIONFicin forms with different casein specificities are present in different proportions during fruit ripening, which is of importance for applications in the dairy industry. The protection mechanism against insects and fungi, which relies on chitinolytic activity, is the most important in the early phases of flowering and is replaced with other strategies over time.
PB  - Wiley, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening
EP  - 582
IS  - 2
SP  - 576
VL  - 96
DO  - 10.1002/jsfa.7126
ER  - 

@article{
author = "Rasković, Brankica and Lazić, Jelena and Polović, Natalija",
year = "2016",
abstract = "BACKGROUNDThe physiological role of fig latex is to protect the plant from pathogens. Latex is a rich source of proteases, predominantly ficin. Fig latex also contains collagenolytic protease and chitinolytic enzymes. Our aim was to investigate changes in protein composition, enzyme and antifungal activities of fig latex during fruit ripening. RESULTSComparison of latex samples in different time periods showed a uniform increase of protein concentration in chronological order. The content of collagenolytic protease did not differ significantly in the latex samples, while the content of ficin decreased. Ficin-specific activity towards casein was the highest at the beginning of fruit development (about 80 U mg(-1)). Specific milk clotting activity increased as well as the abundance of casein band in the clots. Specific chitinolytic activity at the beginning of flowering was 6.5 times higher than the activity in the period when fruits are ripe. Antifungal activity is the most extensive in spring. CONCLUSIONFicin forms with different casein specificities are present in different proportions during fruit ripening, which is of importance for applications in the dairy industry. The protection mechanism against insects and fungi, which relies on chitinolytic activity, is the most important in the early phases of flowering and is replaced with other strategies over time.",
publisher = "Wiley, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening",
pages = "582-576",
number = "2",
volume = "96",
doi = "10.1002/jsfa.7126"
}

Rasković, B., Lazić, J.,& Polović, N.. (2016). Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening. in Journal of the Science of Food and Agriculture
Wiley, Hoboken., 96(2), 576-582.
https://doi.org/10.1002/jsfa.7126

Rasković B, Lazić J, Polović N. Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening. in Journal of the Science of Food and Agriculture. 2016;96(2):576-582.
doi:10.1002/jsfa.7126 .

Rasković, Brankica, Lazić, Jelena, Polović, Natalija, "Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening" in Journal of the Science of Food and Agriculture, 96, no. 2 (2016):576-582,
https://doi.org/10.1002/jsfa.7126 . .

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 . .