Exploring the antibacterial potential of Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 by genome mining, bacteriocin gene overexpression, and chemical protein synthesis of lactolisterin BU variants
Samo za registrovane korisnike
2023
Autori
Malešević, MilkaGardijan, Lazar
Miljković, Marija
O'Connor, Paula M
Mirković, Nemanja
Jovčić, Branko
Cotter, Paul D
Jovanovic, Goran
Kojić, Milan
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
Lactic acid bacterium Lactococcus lactis BGBU1-4 produces 43 amino acids (aa) long bacteriocin, lactolisterin BU (LBU), a 5.161 kDa peptide with potent antibacterial activity against many Gram-positive pathogens. In addition, BGBU1-4 produces an additional unknown product of 3.642 kDa with antibacterial activity. Here, we determined that the significant amount of naturally produced LBU breaks down to create a 3.642 kDa truncated form of LBU bacteriocin consisting of 31 N-terminal aa (LBU1-31) that exhibits 12.5% the antibacterial activity of the full-length LBU. We showed that chemically synthesized LBU is stable and 50% less active than native LBU, and so we used the synthetic peptides of LBU and its variants to further study their activities and antibacterial potential. Deletion analysis of LBU revealed that the 24 N-terminal aa of LBU (LBU1-24) are responsible for antibacterial activity, while downstream aa (25–43) determine the species-specific effectiveness of LBU. Although LBU1-3...1 contains aa 1–24, the truncation at position 31 is predicted to change the structure within aa 15–31 and might impact on antibacterial activity. Intriguingly, whole genome sequencing and genome mining established that BGBU1-4 is abundant in genes that encode potential antibacterials, but produces LBU and its breakdown product LBU1-31 exclusively.
Izvor:
Letters in Applied Microbiology, 2023, 76, 2, ovad004-Finansiranje / projekti:
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200042 (Univerzitet u Beogradu, Institut za molekularnu genetiku i genetičko inženjerstvo) (RS-MESTD-inst-2020-200042)
Institucija/grupa
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Malešević, Milka AU - Gardijan, Lazar AU - Miljković, Marija AU - O'Connor, Paula M AU - Mirković, Nemanja AU - Jovčić, Branko AU - Cotter, Paul D AU - Jovanovic, Goran AU - Kojić, Milan PY - 2023 UR - https://doi.org/10.1093/lambio/ovad004 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/1828 AB - Lactic acid bacterium Lactococcus lactis BGBU1-4 produces 43 amino acids (aa) long bacteriocin, lactolisterin BU (LBU), a 5.161 kDa peptide with potent antibacterial activity against many Gram-positive pathogens. In addition, BGBU1-4 produces an additional unknown product of 3.642 kDa with antibacterial activity. Here, we determined that the significant amount of naturally produced LBU breaks down to create a 3.642 kDa truncated form of LBU bacteriocin consisting of 31 N-terminal aa (LBU1-31) that exhibits 12.5% the antibacterial activity of the full-length LBU. We showed that chemically synthesized LBU is stable and 50% less active than native LBU, and so we used the synthetic peptides of LBU and its variants to further study their activities and antibacterial potential. Deletion analysis of LBU revealed that the 24 N-terminal aa of LBU (LBU1-24) are responsible for antibacterial activity, while downstream aa (25–43) determine the species-specific effectiveness of LBU. Although LBU1-31 contains aa 1–24, the truncation at position 31 is predicted to change the structure within aa 15–31 and might impact on antibacterial activity. Intriguingly, whole genome sequencing and genome mining established that BGBU1-4 is abundant in genes that encode potential antibacterials, but produces LBU and its breakdown product LBU1-31 exclusively. T2 - Letters in Applied Microbiology T2 - Letters in Applied MicrobiologyLetters in Applied Microbiology T1 - Exploring the antibacterial potential of Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 by genome mining, bacteriocin gene overexpression, and chemical protein synthesis of lactolisterin BU variants IS - 2 SP - ovad004 VL - 76 DO - 10.1093/lambio/ovad004 ER -
@article{ author = "Malešević, Milka and Gardijan, Lazar and Miljković, Marija and O'Connor, Paula M and Mirković, Nemanja and Jovčić, Branko and Cotter, Paul D and Jovanovic, Goran and Kojić, Milan", year = "2023", abstract = "Lactic acid bacterium Lactococcus lactis BGBU1-4 produces 43 amino acids (aa) long bacteriocin, lactolisterin BU (LBU), a 5.161 kDa peptide with potent antibacterial activity against many Gram-positive pathogens. In addition, BGBU1-4 produces an additional unknown product of 3.642 kDa with antibacterial activity. Here, we determined that the significant amount of naturally produced LBU breaks down to create a 3.642 kDa truncated form of LBU bacteriocin consisting of 31 N-terminal aa (LBU1-31) that exhibits 12.5% the antibacterial activity of the full-length LBU. We showed that chemically synthesized LBU is stable and 50% less active than native LBU, and so we used the synthetic peptides of LBU and its variants to further study their activities and antibacterial potential. Deletion analysis of LBU revealed that the 24 N-terminal aa of LBU (LBU1-24) are responsible for antibacterial activity, while downstream aa (25–43) determine the species-specific effectiveness of LBU. Although LBU1-31 contains aa 1–24, the truncation at position 31 is predicted to change the structure within aa 15–31 and might impact on antibacterial activity. Intriguingly, whole genome sequencing and genome mining established that BGBU1-4 is abundant in genes that encode potential antibacterials, but produces LBU and its breakdown product LBU1-31 exclusively.", journal = "Letters in Applied Microbiology, Letters in Applied MicrobiologyLetters in Applied Microbiology", title = "Exploring the antibacterial potential of Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 by genome mining, bacteriocin gene overexpression, and chemical protein synthesis of lactolisterin BU variants", number = "2", pages = "ovad004", volume = "76", doi = "10.1093/lambio/ovad004" }
Malešević, M., Gardijan, L., Miljković, M., O'Connor, P. M., Mirković, N., Jovčić, B., Cotter, P. D., Jovanovic, G.,& Kojić, M.. (2023). Exploring the antibacterial potential of Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 by genome mining, bacteriocin gene overexpression, and chemical protein synthesis of lactolisterin BU variants. in Letters in Applied Microbiology, 76(2), ovad004. https://doi.org/10.1093/lambio/ovad004
Malešević M, Gardijan L, Miljković M, O'Connor PM, Mirković N, Jovčić B, Cotter PD, Jovanovic G, Kojić M. Exploring the antibacterial potential of Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 by genome mining, bacteriocin gene overexpression, and chemical protein synthesis of lactolisterin BU variants. in Letters in Applied Microbiology. 2023;76(2):ovad004. doi:10.1093/lambio/ovad004 .
Malešević, Milka, Gardijan, Lazar, Miljković, Marija, O'Connor, Paula M, Mirković, Nemanja, Jovčić, Branko, Cotter, Paul D, Jovanovic, Goran, Kojić, Milan, "Exploring the antibacterial potential of Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 by genome mining, bacteriocin gene overexpression, and chemical protein synthesis of lactolisterin BU variants" in Letters in Applied Microbiology, 76, no. 2 (2023):ovad004, https://doi.org/10.1093/lambio/ovad004 . .