دورية أكاديمية

Selection of escherichia coli heat-labile toxin (LT) inhibitors using both the gm1-elisa and the cAMP Vero cell assay

التفاصيل البيبلوغرافية
العنوان: Selection of escherichia coli heat-labile toxin (LT) inhibitors using both the gm1-elisa and the cAMP Vero cell assay
المؤلفون: Verhelst, R., Schroyen, Martine, Buys, N., Niewold, T.
المصدر: Foodborne Pathogens and Disease, 10 (7), 603-607 (2013)
بيانات النشر: Mary Ann Liebert
سنة النشر: 2013
المجموعة: University of Liège: ORBi (Open Repository and Bibliography)
مصطلحات موضوعية: Escherichia coli protein, Escherichia coli, Vero cell, Abrus, Canavalia, Chlorocebus aethiops, Escherichia coli Infections, Fabaceae, Swine Diseases, Vero cell line, Animalia, Acetylgalactosamine, Animals, Bacterial Toxins, Cell Survival, Cercopithecus aethiops, Diarrhea, Enterotoxigenic Escherichia coli, Enterotoxins, Enzyme-Linked Immunosorbent Assay, Escherichia coli Proteins, Galactose, Humans, Lactose, Plant Extracts, Polyphenols, Protein Binding, Receptors, Cell Surface, Swine
الوصف: peer reviewed ; Weaned piglets are very susceptible to diarrhea caused by enterotoxigenic Escherichia coli. In the past, various natural components were proposed to have beneficial effects by reducing the effects of diarrheal infectious diseases in humans and animals, and thus may represent an alternative for the use of (prophylactic) antibiotics. Alternatives may inactivate enterotoxigenic Escherichia coli heat-labile toxin (LT) by interfering with toxin binding to the cellular receptor GM1. In this study, various plants and other natural substances were tested for inhibitory properties, in the GM1 binding assay, and in the LT-induced cAMP production in Vero cells. The toxic dose of each compound was determined in a cell viability assay, and the highest nontoxic concentrations were used in the GM1 and cAMP assays. Results demonstrated that only d-(+)-galactose, lactose, N-acetyl-d-galactosamine, and two tea extracts were able to inhibit the binding of LT to its GM1 receptor. In the cAMP assay, only the two tea extracts showed inhibitory activity. This shows that d-(+)-galactose, lactose, and N-acetyl-d-galactosamine can indeed inhibit LT binding to GM1 based on structural homology with GM1 in the absence of living cells. However, in the cAMP assay, d-(+)-galactose, and lactose, N-acetyl-d-galactosamine are apparently metabolized to below their effective inhibitory concentration, likely predicting limited practical applicability in vivo. Both tea extracts maintained their activity in the presence of cells. The active compounds in both are probably polyphenols, which are not easily metabolized, and most likely work by aggregating the toxin. In conclusion, the combination of methods used here is a convenient and fast method for preselecting natural substances containing potentially toxin-binding compounds. Furthermore, if antidiarrhea activity is attributed to compounds found inactive here, their activity is unlikely based on interference with toxin binding. © Copyright 2013, Mary Ann Liebert, Inc. 2013.
نوع الوثيقة: article in journal/newspaper
اللغة: unknown
تدمد: 1535-3141
1556-7125
العلاقة: urn:issn:1535-3141; urn:issn:1556-7125; https://orbi.uliege.be/handle/2268/209868Test; info:hdl:2268/209868; scopus-id:2-s2.0-84879565025; info:pmid:23692076
DOI: 10.1089/fpd.2012.1434
الإتاحة: https://doi.org/10.1089/fpd.2012.1434Test
https://orbi.uliege.be/handle/2268/209868Test
حقوق: restricted access ; http://purl.org/coar/access_right/c_16ecTest ; info:eu-repo/semantics/restrictedAccess
رقم الانضمام: edsbas.C6DF460A
قاعدة البيانات: BASE
الوصف
تدمد:15353141
15567125
DOI:10.1089/fpd.2012.1434