Aggregation Factor as an Inhibitor of Bacterial Binding to Gut Mucosa
Само за регистроване кориснике
2014
Аутори
Lukić, JovankaStrahinić, Ivana
Milenković, Marina
Živković, Milica
Tolinački, Maja
Kojić, Milan
Begović, Jelena
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Modern research in the area of probiotics is largely devoted to discovering factors that promote the adherence of probiotic candidates to host mucosal surfaces. The aim of the present study was to test the role of aggregation factor (AggL) and mucin-binding protein (MbpL) from Lactococcus sp. in adhesion to gastrointestinal mucosa. In vitro, ex vivo, and in vivo experiments in rats were used to assess the adhesive potential of these two proteins expressed in heterologous host Lactobacillus salivarius BGHO1. Although there was no influence of MbpL protein expression on BGHO1 adhesion to gut mucosa, expression of AggL had a negative effect on BGHO1 binding to ileal and colonic rat mucosa, as well as to human HT29-MTX cells and porcine gastric mucin in vitro. Because AggL did not decrease the adhesion of bacteria to intestinal fragments in ex vivo tests, where peristaltic simulation conditions were missing, we propose that intestinal motility could be a crucial force for eliminating aggre...gation-factor-bearing bacteria. Bacterial strains expressing aggregation factor could facilitate the removal of pathogens through the coaggregation mechanism, thus balancing gut microbial ecosystems in people affected by intestinal bacteria overgrowth.
Извор:
Microbial Ecology, 2014, 68, 3, 633-644Издавач:
- Springer, New York
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: 10.1007/s00248-014-0426-1
ISSN: 0095-3628
PubMed: 24823989
WoS: 000342204100019
Scopus: 2-s2.0-84907696949
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Lukić, Jovanka AU - Strahinić, Ivana AU - Milenković, Marina AU - Živković, Milica AU - Tolinački, Maja AU - Kojić, Milan AU - Begović, Jelena PY - 2014 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/748 AB - Modern research in the area of probiotics is largely devoted to discovering factors that promote the adherence of probiotic candidates to host mucosal surfaces. The aim of the present study was to test the role of aggregation factor (AggL) and mucin-binding protein (MbpL) from Lactococcus sp. in adhesion to gastrointestinal mucosa. In vitro, ex vivo, and in vivo experiments in rats were used to assess the adhesive potential of these two proteins expressed in heterologous host Lactobacillus salivarius BGHO1. Although there was no influence of MbpL protein expression on BGHO1 adhesion to gut mucosa, expression of AggL had a negative effect on BGHO1 binding to ileal and colonic rat mucosa, as well as to human HT29-MTX cells and porcine gastric mucin in vitro. Because AggL did not decrease the adhesion of bacteria to intestinal fragments in ex vivo tests, where peristaltic simulation conditions were missing, we propose that intestinal motility could be a crucial force for eliminating aggregation-factor-bearing bacteria. Bacterial strains expressing aggregation factor could facilitate the removal of pathogens through the coaggregation mechanism, thus balancing gut microbial ecosystems in people affected by intestinal bacteria overgrowth. PB - Springer, New York T2 - Microbial Ecology T1 - Aggregation Factor as an Inhibitor of Bacterial Binding to Gut Mucosa EP - 644 IS - 3 SP - 633 VL - 68 DO - 10.1007/s00248-014-0426-1 ER -
@article{ author = "Lukić, Jovanka and Strahinić, Ivana and Milenković, Marina and Živković, Milica and Tolinački, Maja and Kojić, Milan and Begović, Jelena", year = "2014", abstract = "Modern research in the area of probiotics is largely devoted to discovering factors that promote the adherence of probiotic candidates to host mucosal surfaces. The aim of the present study was to test the role of aggregation factor (AggL) and mucin-binding protein (MbpL) from Lactococcus sp. in adhesion to gastrointestinal mucosa. In vitro, ex vivo, and in vivo experiments in rats were used to assess the adhesive potential of these two proteins expressed in heterologous host Lactobacillus salivarius BGHO1. Although there was no influence of MbpL protein expression on BGHO1 adhesion to gut mucosa, expression of AggL had a negative effect on BGHO1 binding to ileal and colonic rat mucosa, as well as to human HT29-MTX cells and porcine gastric mucin in vitro. Because AggL did not decrease the adhesion of bacteria to intestinal fragments in ex vivo tests, where peristaltic simulation conditions were missing, we propose that intestinal motility could be a crucial force for eliminating aggregation-factor-bearing bacteria. Bacterial strains expressing aggregation factor could facilitate the removal of pathogens through the coaggregation mechanism, thus balancing gut microbial ecosystems in people affected by intestinal bacteria overgrowth.", publisher = "Springer, New York", journal = "Microbial Ecology", title = "Aggregation Factor as an Inhibitor of Bacterial Binding to Gut Mucosa", pages = "644-633", number = "3", volume = "68", doi = "10.1007/s00248-014-0426-1" }
Lukić, J., Strahinić, I., Milenković, M., Živković, M., Tolinački, M., Kojić, M.,& Begović, J.. (2014). Aggregation Factor as an Inhibitor of Bacterial Binding to Gut Mucosa. in Microbial Ecology Springer, New York., 68(3), 633-644. https://doi.org/10.1007/s00248-014-0426-1
Lukić J, Strahinić I, Milenković M, Živković M, Tolinački M, Kojić M, Begović J. Aggregation Factor as an Inhibitor of Bacterial Binding to Gut Mucosa. in Microbial Ecology. 2014;68(3):633-644. doi:10.1007/s00248-014-0426-1 .
Lukić, Jovanka, Strahinić, Ivana, Milenković, Marina, Živković, Milica, Tolinački, Maja, Kojić, Milan, Begović, Jelena, "Aggregation Factor as an Inhibitor of Bacterial Binding to Gut Mucosa" in Microbial Ecology, 68, no. 3 (2014):633-644, https://doi.org/10.1007/s00248-014-0426-1 . .