Cloning and expression of a novel lactococcal aggregation factor from Lactococcus lactis subsp lactis BGKP1
Аутори
Kojić, MilanJovčić, Branko
Strahinić, Ivana
Begović, Jelena
Lozo, Jelena
Veljović, Katarina
Topisirović, Ljubiša
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Background: Aggregation may play a main role in the adhesion of bacteria to the gastrointestinal epithelium and their colonization ability, as well as in probiotic effects through co-aggregation with intestinal pathogens and their subsequent removal. The aggregation phenomenon in lactococci is directly associated with the sex factor and lactose plasmid co-integration event or duplication of the cell wall spanning (CWS) domain of PrtP proteinase. Results: Lactococcus lactis subsp. lactis BGKP1 was isolated from artisanal semi-hard homemade cheese and selected due to its strong auto-aggregation phenotype. Subsequently, non-aggregating derivative (Agg(-)) of BGKP1, designated as BGKP1-20, was isolated, too. Comparative analysis of cell surface proteins of BGKP1 and derivative BGKP1-20 revealed a protein of approximately 200 kDa only in the parental strain BGKP1. The gene involved in aggregation (aggL) was mapped on plasmid pKP1 (16.2 kb), cloned and expressed in homologous and heterologou...s lactococci and enterococci. This novel lactococcal aggregation protein was shown to be sufficient for cell aggregation in all tested hosts. In addition to the aggL gene, six more ORFs involved in replication (repB and repX), restriction and modification (hsdS), transposition (tnp) and possible interaction with mucin (mbpL) were also located on plasmid pKP1. Conclusion: AggL is a new protein belonging to the collagen-binding superfamily of proteins and is sufficient for cell aggregation in lactococci.
Извор:
BMC Microbiology, 2011, 11Издавач:
- Biomed Central Ltd, London
Финансирање / пројекти:
- Изучавање гена и молекуларних механизама у основи пробиотичке активности бактерија млечне киселине изолованих са подручја западног Балкана (RS-MESTD-Basic Research (BR or ON)-173019)
- International Centre of Genetic Engineering and Biotechnology, Italy [CRP-YUG10-01]
DOI: 10.1186/1471-2180-11-265
ISSN: 1471-2180
PubMed: 22182285
WoS: 000300434800001
Scopus: 2-s2.0-83655182584
Институција/група
TorlakTY - JOUR AU - Kojić, Milan AU - Jovčić, Branko AU - Strahinić, Ivana AU - Begović, Jelena AU - Lozo, Jelena AU - Veljović, Katarina AU - Topisirović, Ljubiša PY - 2011 UR - http://intor.torlakinstitut.com/handle/123456789/723 AB - Background: Aggregation may play a main role in the adhesion of bacteria to the gastrointestinal epithelium and their colonization ability, as well as in probiotic effects through co-aggregation with intestinal pathogens and their subsequent removal. The aggregation phenomenon in lactococci is directly associated with the sex factor and lactose plasmid co-integration event or duplication of the cell wall spanning (CWS) domain of PrtP proteinase. Results: Lactococcus lactis subsp. lactis BGKP1 was isolated from artisanal semi-hard homemade cheese and selected due to its strong auto-aggregation phenotype. Subsequently, non-aggregating derivative (Agg(-)) of BGKP1, designated as BGKP1-20, was isolated, too. Comparative analysis of cell surface proteins of BGKP1 and derivative BGKP1-20 revealed a protein of approximately 200 kDa only in the parental strain BGKP1. The gene involved in aggregation (aggL) was mapped on plasmid pKP1 (16.2 kb), cloned and expressed in homologous and heterologous lactococci and enterococci. This novel lactococcal aggregation protein was shown to be sufficient for cell aggregation in all tested hosts. In addition to the aggL gene, six more ORFs involved in replication (repB and repX), restriction and modification (hsdS), transposition (tnp) and possible interaction with mucin (mbpL) were also located on plasmid pKP1. Conclusion: AggL is a new protein belonging to the collagen-binding superfamily of proteins and is sufficient for cell aggregation in lactococci. PB - Biomed Central Ltd, London T2 - BMC Microbiology T1 - Cloning and expression of a novel lactococcal aggregation factor from Lactococcus lactis subsp lactis BGKP1 VL - 11 DO - 10.1186/1471-2180-11-265 ER -
@article{ author = "Kojić, Milan and Jovčić, Branko and Strahinić, Ivana and Begović, Jelena and Lozo, Jelena and Veljović, Katarina and Topisirović, Ljubiša", year = "2011", abstract = "Background: Aggregation may play a main role in the adhesion of bacteria to the gastrointestinal epithelium and their colonization ability, as well as in probiotic effects through co-aggregation with intestinal pathogens and their subsequent removal. The aggregation phenomenon in lactococci is directly associated with the sex factor and lactose plasmid co-integration event or duplication of the cell wall spanning (CWS) domain of PrtP proteinase. Results: Lactococcus lactis subsp. lactis BGKP1 was isolated from artisanal semi-hard homemade cheese and selected due to its strong auto-aggregation phenotype. Subsequently, non-aggregating derivative (Agg(-)) of BGKP1, designated as BGKP1-20, was isolated, too. Comparative analysis of cell surface proteins of BGKP1 and derivative BGKP1-20 revealed a protein of approximately 200 kDa only in the parental strain BGKP1. The gene involved in aggregation (aggL) was mapped on plasmid pKP1 (16.2 kb), cloned and expressed in homologous and heterologous lactococci and enterococci. This novel lactococcal aggregation protein was shown to be sufficient for cell aggregation in all tested hosts. In addition to the aggL gene, six more ORFs involved in replication (repB and repX), restriction and modification (hsdS), transposition (tnp) and possible interaction with mucin (mbpL) were also located on plasmid pKP1. Conclusion: AggL is a new protein belonging to the collagen-binding superfamily of proteins and is sufficient for cell aggregation in lactococci.", publisher = "Biomed Central Ltd, London", journal = "BMC Microbiology", title = "Cloning and expression of a novel lactococcal aggregation factor from Lactococcus lactis subsp lactis BGKP1", volume = "11", doi = "10.1186/1471-2180-11-265" }
Kojić, M., Jovčić, B., Strahinić, I., Begović, J., Lozo, J., Veljović, K.,& Topisirović, L.. (2011). Cloning and expression of a novel lactococcal aggregation factor from Lactococcus lactis subsp lactis BGKP1. in BMC Microbiology Biomed Central Ltd, London., 11. https://doi.org/10.1186/1471-2180-11-265
Kojić M, Jovčić B, Strahinić I, Begović J, Lozo J, Veljović K, Topisirović L. Cloning and expression of a novel lactococcal aggregation factor from Lactococcus lactis subsp lactis BGKP1. in BMC Microbiology. 2011;11. doi:10.1186/1471-2180-11-265 .
Kojić, Milan, Jovčić, Branko, Strahinić, Ivana, Begović, Jelena, Lozo, Jelena, Veljović, Katarina, Topisirović, Ljubiša, "Cloning and expression of a novel lactococcal aggregation factor from Lactococcus lactis subsp lactis BGKP1" in BMC Microbiology, 11 (2011), https://doi.org/10.1186/1471-2180-11-265 . .