TY  - JOUR
AU  - Malešević, Milka
AU  - Stanisavljević, Nemanja S.
AU  - Novović, Katarina
AU  - Polović, Natalija
AU  - Vasiljević, Zorica
AU  - Kojić, Milan O.
AU  - Jovčić, Branko
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4257
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  - Elsevier
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 S. and Novović, Katarina and Polović, Natalija and Vasiljević, Zorica and Kojić, Milan O. 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 = "Elsevier",
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. S., Novović, K., Polović, N., Vasiljević, Z., Kojić, M. O.,& Jovčić, B.. (2020). Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity. in Microbial Pathogenesis
Elsevier., 149.
https://doi.org/10.1016/j.micpath.2020.104561

Malešević M, Stanisavljević NS, Novović K, Polović N, Vasiljević Z, Kojić MO, 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 S., Novović, Katarina, Polović, Natalija, Vasiljević, Zorica, Kojić, Milan O., 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  - Klisurić, Olivera
AU  - Armaković, Sanja J.
AU  - Armaković, Stevan
AU  - Marković, Sanja B.
AU  - Todorović, Tamara
AU  - Portalone, Gustavo
AU  - Novović, Katarina
AU  - Lozo, Jelena
AU  - Filipović, Nenad R.
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3801
AB  - In this work pharmaceutical application of focused library of six quinoline-based chalcogensemicarbazones (QBCs) was tested through determination of their antimicrobial activity against twenty-eight Gram-negative and Gram-positive strains from different origin. Pharmacokinetic properties have been assessed by the analysis of frequently employed drug likeness parameters. Computational study has been complemented with calculation of their global and local reactive properties, within the framework of density functional theory (DFT). Among other information, DFT calculations helped us to locate the most reactive sites of investigated QBCs and to identify their sensitivity towards the oxidation.
PB  - Elsevier
T2  - Journal of Molecular Structure
T1  - Structural, biological and in-silico study of quinoline-based chalcogensemicarbazones
VL  - 1203
SP  - 127482
DO  - 10.1016/j.molstruc.2019.127482
ER  - 

@article{
author = "Klisurić, Olivera and Armaković, Sanja J. and Armaković, Stevan and Marković, Sanja B. and Todorović, Tamara and Portalone, Gustavo and Novović, Katarina and Lozo, Jelena and Filipović, Nenad R.",
year = "2020",
abstract = "In this work pharmaceutical application of focused library of six quinoline-based chalcogensemicarbazones (QBCs) was tested through determination of their antimicrobial activity against twenty-eight Gram-negative and Gram-positive strains from different origin. Pharmacokinetic properties have been assessed by the analysis of frequently employed drug likeness parameters. Computational study has been complemented with calculation of their global and local reactive properties, within the framework of density functional theory (DFT). Among other information, DFT calculations helped us to locate the most reactive sites of investigated QBCs and to identify their sensitivity towards the oxidation.",
publisher = "Elsevier",
journal = "Journal of Molecular Structure",
title = "Structural, biological and in-silico study of quinoline-based chalcogensemicarbazones",
volume = "1203",
pages = "127482",
doi = "10.1016/j.molstruc.2019.127482"
}

Klisurić, O., Armaković, S. J., Armaković, S., Marković, S. B., Todorović, T., Portalone, G., Novović, K., Lozo, J.,& Filipović, N. R.. (2020). Structural, biological and in-silico study of quinoline-based chalcogensemicarbazones. in Journal of Molecular Structure
Elsevier., 1203, 127482.
https://doi.org/10.1016/j.molstruc.2019.127482

Klisurić O, Armaković SJ, Armaković S, Marković SB, Todorović T, Portalone G, Novović K, Lozo J, Filipović NR. Structural, biological and in-silico study of quinoline-based chalcogensemicarbazones. in Journal of Molecular Structure. 2020;1203:127482.
doi:10.1016/j.molstruc.2019.127482 .

Klisurić, Olivera, Armaković, Sanja J., Armaković, Stevan, Marković, Sanja B., Todorović, Tamara, Portalone, Gustavo, Novović, Katarina, Lozo, Jelena, Filipović, Nenad R., "Structural, biological and in-silico study of quinoline-based chalcogensemicarbazones" in Journal of Molecular Structure, 1203 (2020):127482,
https://doi.org/10.1016/j.molstruc.2019.127482 . .