Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation
2016
Аутори
Miljković, MarijaBertani, Iris
Fira, Đorđe
Jovčić, Branko
Novović, Katarina
Venturi, Vittorio
Kojić, Milan
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
AggLb is the largest (318.6 kDa) aggregation-promoting protein of Lactobacillus paracasei subsp. paracasei BGNJ1-64 responsible for forming large cell aggregates, which causes auto-aggregation, collagen binding and pathogen exclusion in vitro. It contains an N-terminus leader peptide, followed by six successive collagen binding domains, 20 successive repeats (CnaB-like domains) and an LPXTG sorting signal at the C-terminus for cell wall anchoring. Experimental information about the roles of the domains of AggLb is currently unknown. To define the domain that confers cell aggregation and the key domains for interactions of specific affinity between AggLb and components of the extracellular matrix, we constructed a series of variants of the aggLb gene and expressed them in Lactococcus lactis subsp. lactis BGKP1-20 using a lactococcal promoter. All of the variants contained a leader peptide, an inter collagen binding-CnaB domain region (used to raise an anti-AggLb antibody), an anchor dom...ain and a different number of collagen binding and CnaB-like domains. The role of the collagen binding repeats of the N-terminus in auto-aggregation and binding to collagen and fibronectin was confirmed. Deletion of the collagen binding repeats II, III, and IV resulted in a loss of the strong auto-aggregation, collagen and fibronectin binding abilities whereas the biofilm formation capability was increased. The strong auto-aggregation, collagen and fibronectin binding abilities of AggLb were negatively correlated to biofilm formation.
Кључне речи:
collagen binding domains / CnaB-like domains / biofilm formation / auto-aggregation / AggLbИзвор:
Frontiers in Microbiology, 2016, 7, 1-14Издавач:
- Frontiers Media Sa, Lausanne
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)
DOI: 10.3389/fmicb.2016.01422
ISSN: 1664-302X
WoS: 000382818700001
Scopus: 2-s2.0-84992754205
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Miljković, Marija AU - Bertani, Iris AU - Fira, Đorđe AU - Jovčić, Branko AU - Novović, Katarina AU - Venturi, Vittorio AU - Kojić, Milan PY - 2016 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/924 AB - AggLb is the largest (318.6 kDa) aggregation-promoting protein of Lactobacillus paracasei subsp. paracasei BGNJ1-64 responsible for forming large cell aggregates, which causes auto-aggregation, collagen binding and pathogen exclusion in vitro. It contains an N-terminus leader peptide, followed by six successive collagen binding domains, 20 successive repeats (CnaB-like domains) and an LPXTG sorting signal at the C-terminus for cell wall anchoring. Experimental information about the roles of the domains of AggLb is currently unknown. To define the domain that confers cell aggregation and the key domains for interactions of specific affinity between AggLb and components of the extracellular matrix, we constructed a series of variants of the aggLb gene and expressed them in Lactococcus lactis subsp. lactis BGKP1-20 using a lactococcal promoter. All of the variants contained a leader peptide, an inter collagen binding-CnaB domain region (used to raise an anti-AggLb antibody), an anchor domain and a different number of collagen binding and CnaB-like domains. The role of the collagen binding repeats of the N-terminus in auto-aggregation and binding to collagen and fibronectin was confirmed. Deletion of the collagen binding repeats II, III, and IV resulted in a loss of the strong auto-aggregation, collagen and fibronectin binding abilities whereas the biofilm formation capability was increased. The strong auto-aggregation, collagen and fibronectin binding abilities of AggLb were negatively correlated to biofilm formation. PB - Frontiers Media Sa, Lausanne T2 - Frontiers in Microbiology T1 - Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation EP - 14 SP - 1 VL - 7 DO - 10.3389/fmicb.2016.01422 ER -
@article{ author = "Miljković, Marija and Bertani, Iris and Fira, Đorđe and Jovčić, Branko and Novović, Katarina and Venturi, Vittorio and Kojić, Milan", year = "2016", abstract = "AggLb is the largest (318.6 kDa) aggregation-promoting protein of Lactobacillus paracasei subsp. paracasei BGNJ1-64 responsible for forming large cell aggregates, which causes auto-aggregation, collagen binding and pathogen exclusion in vitro. It contains an N-terminus leader peptide, followed by six successive collagen binding domains, 20 successive repeats (CnaB-like domains) and an LPXTG sorting signal at the C-terminus for cell wall anchoring. Experimental information about the roles of the domains of AggLb is currently unknown. To define the domain that confers cell aggregation and the key domains for interactions of specific affinity between AggLb and components of the extracellular matrix, we constructed a series of variants of the aggLb gene and expressed them in Lactococcus lactis subsp. lactis BGKP1-20 using a lactococcal promoter. All of the variants contained a leader peptide, an inter collagen binding-CnaB domain region (used to raise an anti-AggLb antibody), an anchor domain and a different number of collagen binding and CnaB-like domains. The role of the collagen binding repeats of the N-terminus in auto-aggregation and binding to collagen and fibronectin was confirmed. Deletion of the collagen binding repeats II, III, and IV resulted in a loss of the strong auto-aggregation, collagen and fibronectin binding abilities whereas the biofilm formation capability was increased. The strong auto-aggregation, collagen and fibronectin binding abilities of AggLb were negatively correlated to biofilm formation.", publisher = "Frontiers Media Sa, Lausanne", journal = "Frontiers in Microbiology", title = "Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation", pages = "14-1", volume = "7", doi = "10.3389/fmicb.2016.01422" }
Miljković, M., Bertani, I., Fira, Đ., Jovčić, B., Novović, K., Venturi, V.,& Kojić, M.. (2016). Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation. in Frontiers in Microbiology Frontiers Media Sa, Lausanne., 7, 1-14. https://doi.org/10.3389/fmicb.2016.01422
Miljković M, Bertani I, Fira Đ, Jovčić B, Novović K, Venturi V, Kojić M. Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation. in Frontiers in Microbiology. 2016;7:1-14. doi:10.3389/fmicb.2016.01422 .
Miljković, Marija, Bertani, Iris, Fira, Đorđe, Jovčić, Branko, Novović, Katarina, Venturi, Vittorio, Kojić, Milan, "Shortening of the Lactobacillus paracasei subsp paracasei BGNJ164 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation" in Frontiers in Microbiology, 7 (2016):1-14, https://doi.org/10.3389/fmicb.2016.01422 . .