AggLb Is the Largest Cell-Aggregation Factor from Lactobacillus paracasei Subsp paracasei BGNJ1-64, Functions in Collagen Adhesion, and Pathogen Exclusion In Vitro
Аутори
Miljković, MarijaStrahinić, Ivana
Tolinački, Maja
Živković, Milica
Kojić, Snežana
Golić, Nataša
Kojić, Milan
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Eleven Lactobacillus strains with strong aggregation abilities were selected from a laboratory collection. In two of the strains, genes associated with aggregation capability were plasmid located and found to strongly correlate with collagen binding. The gene encoding the auto-aggregation-promoting protein (AggLb) of Lactobacillus paracasei subsp. paracasei BGNJ1-64 was cloned using a novel, wide-range-host shuttle cloning vector, pAZILSJ. The clone pALb35, containing a 11377-bp DNA fragment, was selected from the SacI plasmid library for its ability to provide carriers with the aggregation phenotype. The complete fragment was sequenced and four potential ORFs were detected, including the aggLb gene and three surrounding transposase genes. AggLb is the largest known cell-surface protein in lactobacilli, consisting of 2998 aa (318,611 Da). AggLb belongs to the collagen-binding superfamily and its C-terminal region contains 20 successive repeats that are identical even at the nucleotide ...level. Deletion of aggLb causes a loss of the capacity to form cell aggregates, whereas overexpression increases cellular aggregation, hydrophobicity and collagen-binding potential. PCR screening performed with three sets of primers based on the aggLb gene of BGNJ1-64 enabled detection of the same type of aggLb gene in five of eleven selected aggregation-positive Lactobacillus strains. Heterologous expression of aggLb confirmed the crucial role of the AggLb protein in cell aggregation and specific collagen binding, indicating that AggLb has a useful probiotic function in effective colonization of host tissue and prevention of pathogen colonization.
Извор:
PLoS One, 2015, 10, 5Издавач:
- Public Library Science, San Francisco
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: 10.1371/journal.pone.0126387
ISSN: 1932-6203
PubMed: 25955159
WoS: 000356768100115
Scopus: 2-s2.0-84947017406
URI
https://imagine.imgge.bg.ac.rs/handle/123456789/805http://intor.torlakinstitut.com/handle/123456789/685
Институција/група
TorlakTY - JOUR AU - Miljković, Marija AU - Strahinić, Ivana AU - Tolinački, Maja AU - Živković, Milica AU - Kojić, Snežana AU - Golić, Nataša AU - Kojić, Milan PY - 2015 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/805 UR - http://intor.torlakinstitut.com/handle/123456789/685 AB - Eleven Lactobacillus strains with strong aggregation abilities were selected from a laboratory collection. In two of the strains, genes associated with aggregation capability were plasmid located and found to strongly correlate with collagen binding. The gene encoding the auto-aggregation-promoting protein (AggLb) of Lactobacillus paracasei subsp. paracasei BGNJ1-64 was cloned using a novel, wide-range-host shuttle cloning vector, pAZILSJ. The clone pALb35, containing a 11377-bp DNA fragment, was selected from the SacI plasmid library for its ability to provide carriers with the aggregation phenotype. The complete fragment was sequenced and four potential ORFs were detected, including the aggLb gene and three surrounding transposase genes. AggLb is the largest known cell-surface protein in lactobacilli, consisting of 2998 aa (318,611 Da). AggLb belongs to the collagen-binding superfamily and its C-terminal region contains 20 successive repeats that are identical even at the nucleotide level. Deletion of aggLb causes a loss of the capacity to form cell aggregates, whereas overexpression increases cellular aggregation, hydrophobicity and collagen-binding potential. PCR screening performed with three sets of primers based on the aggLb gene of BGNJ1-64 enabled detection of the same type of aggLb gene in five of eleven selected aggregation-positive Lactobacillus strains. Heterologous expression of aggLb confirmed the crucial role of the AggLb protein in cell aggregation and specific collagen binding, indicating that AggLb has a useful probiotic function in effective colonization of host tissue and prevention of pathogen colonization. PB - Public Library Science, San Francisco T2 - PLoS One T1 - AggLb Is the Largest Cell-Aggregation Factor from Lactobacillus paracasei Subsp paracasei BGNJ1-64, Functions in Collagen Adhesion, and Pathogen Exclusion In Vitro IS - 5 VL - 10 DO - 10.1371/journal.pone.0126387 ER -
@article{ author = "Miljković, Marija and Strahinić, Ivana and Tolinački, Maja and Živković, Milica and Kojić, Snežana and Golić, Nataša and Kojić, Milan", year = "2015", abstract = "Eleven Lactobacillus strains with strong aggregation abilities were selected from a laboratory collection. In two of the strains, genes associated with aggregation capability were plasmid located and found to strongly correlate with collagen binding. The gene encoding the auto-aggregation-promoting protein (AggLb) of Lactobacillus paracasei subsp. paracasei BGNJ1-64 was cloned using a novel, wide-range-host shuttle cloning vector, pAZILSJ. The clone pALb35, containing a 11377-bp DNA fragment, was selected from the SacI plasmid library for its ability to provide carriers with the aggregation phenotype. The complete fragment was sequenced and four potential ORFs were detected, including the aggLb gene and three surrounding transposase genes. AggLb is the largest known cell-surface protein in lactobacilli, consisting of 2998 aa (318,611 Da). AggLb belongs to the collagen-binding superfamily and its C-terminal region contains 20 successive repeats that are identical even at the nucleotide level. Deletion of aggLb causes a loss of the capacity to form cell aggregates, whereas overexpression increases cellular aggregation, hydrophobicity and collagen-binding potential. PCR screening performed with three sets of primers based on the aggLb gene of BGNJ1-64 enabled detection of the same type of aggLb gene in five of eleven selected aggregation-positive Lactobacillus strains. Heterologous expression of aggLb confirmed the crucial role of the AggLb protein in cell aggregation and specific collagen binding, indicating that AggLb has a useful probiotic function in effective colonization of host tissue and prevention of pathogen colonization.", publisher = "Public Library Science, San Francisco", journal = "PLoS One", title = "AggLb Is the Largest Cell-Aggregation Factor from Lactobacillus paracasei Subsp paracasei BGNJ1-64, Functions in Collagen Adhesion, and Pathogen Exclusion In Vitro", number = "5", volume = "10", doi = "10.1371/journal.pone.0126387" }
Miljković, M., Strahinić, I., Tolinački, M., Živković, M., Kojić, S., Golić, N.,& Kojić, M.. (2015). AggLb Is the Largest Cell-Aggregation Factor from Lactobacillus paracasei Subsp paracasei BGNJ1-64, Functions in Collagen Adhesion, and Pathogen Exclusion In Vitro. in PLoS One Public Library Science, San Francisco., 10(5). https://doi.org/10.1371/journal.pone.0126387
Miljković M, Strahinić I, Tolinački M, Živković M, Kojić S, Golić N, Kojić M. AggLb Is the Largest Cell-Aggregation Factor from Lactobacillus paracasei Subsp paracasei BGNJ1-64, Functions in Collagen Adhesion, and Pathogen Exclusion In Vitro. in PLoS One. 2015;10(5). doi:10.1371/journal.pone.0126387 .
Miljković, Marija, Strahinić, Ivana, Tolinački, Maja, Živković, Milica, Kojić, Snežana, Golić, Nataša, Kojić, Milan, "AggLb Is the Largest Cell-Aggregation Factor from Lactobacillus paracasei Subsp paracasei BGNJ1-64, Functions in Collagen Adhesion, and Pathogen Exclusion In Vitro" in PLoS One, 10, no. 5 (2015), https://doi.org/10.1371/journal.pone.0126387 . .