Cargando…

Evaluation of inhibition of F4ac positive Escherichia coli attachment with xanthine dehydrogenase, butyrophilin, lactadherin and fatty acid binding protein

BACKGROUND: Neonatal and post-weaning colibacillosis caused by enterotoxigenic E. coli is responsible for substantial economic losses encountered by the pork industry. Intestinal colonization of young piglets by E. coli depends on the efficiency of bacterial attachment to host gastrointestinal epith...

Descripción completa

Detalles Bibliográficos
Autores principales: Novakovic, Predrag, Charavaryamath, Chandrashekhar, Moshynskyy, Igor, Lockerbie, Betty, Kaushik, Radhey S., Loewen, Matthew E., Kidney, Beverly A., Stuart, Chris, Simko, Elemir
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571123/
https://www.ncbi.nlm.nih.gov/pubmed/26374102
http://dx.doi.org/10.1186/s12917-015-0528-0
_version_ 1782390306565521408
author Novakovic, Predrag
Charavaryamath, Chandrashekhar
Moshynskyy, Igor
Lockerbie, Betty
Kaushik, Radhey S.
Loewen, Matthew E.
Kidney, Beverly A.
Stuart, Chris
Simko, Elemir
author_facet Novakovic, Predrag
Charavaryamath, Chandrashekhar
Moshynskyy, Igor
Lockerbie, Betty
Kaushik, Radhey S.
Loewen, Matthew E.
Kidney, Beverly A.
Stuart, Chris
Simko, Elemir
author_sort Novakovic, Predrag
collection PubMed
description BACKGROUND: Neonatal and post-weaning colibacillosis caused by enterotoxigenic E. coli is responsible for substantial economic losses encountered by the pork industry. Intestinal colonization of young piglets by E. coli depends on the efficiency of bacterial attachment to host gastrointestinal epithelium that is mediated by fimbriae. We tested the effect of porcine individual milk fat globule membrane (MFGM) proteins on F4ac positive E. coli attachment to porcine enterocytes in vitro. RESULTS: Butyrophilin, lactadherin and fatty acid binding protein inhibited fimbriae-dependent adherence of E. coli to enterocytes in vitro, while xanthine dehydrogenase did not. The inhibiting activity was dose-dependent for all three proteins, but the inhibiting efficiency was different. CONCLUSIONS: The results indicate that MFGM proteins may interfere with attachment of E. coli to porcine neonatal intestinal mucosa.
format Online
Article
Text
id pubmed-4571123
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-45711232015-09-17 Evaluation of inhibition of F4ac positive Escherichia coli attachment with xanthine dehydrogenase, butyrophilin, lactadherin and fatty acid binding protein Novakovic, Predrag Charavaryamath, Chandrashekhar Moshynskyy, Igor Lockerbie, Betty Kaushik, Radhey S. Loewen, Matthew E. Kidney, Beverly A. Stuart, Chris Simko, Elemir BMC Vet Res Research Article BACKGROUND: Neonatal and post-weaning colibacillosis caused by enterotoxigenic E. coli is responsible for substantial economic losses encountered by the pork industry. Intestinal colonization of young piglets by E. coli depends on the efficiency of bacterial attachment to host gastrointestinal epithelium that is mediated by fimbriae. We tested the effect of porcine individual milk fat globule membrane (MFGM) proteins on F4ac positive E. coli attachment to porcine enterocytes in vitro. RESULTS: Butyrophilin, lactadherin and fatty acid binding protein inhibited fimbriae-dependent adherence of E. coli to enterocytes in vitro, while xanthine dehydrogenase did not. The inhibiting activity was dose-dependent for all three proteins, but the inhibiting efficiency was different. CONCLUSIONS: The results indicate that MFGM proteins may interfere with attachment of E. coli to porcine neonatal intestinal mucosa. BioMed Central 2015-09-15 /pmc/articles/PMC4571123/ /pubmed/26374102 http://dx.doi.org/10.1186/s12917-015-0528-0 Text en © Novakovic et al. 2015 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Novakovic, Predrag
Charavaryamath, Chandrashekhar
Moshynskyy, Igor
Lockerbie, Betty
Kaushik, Radhey S.
Loewen, Matthew E.
Kidney, Beverly A.
Stuart, Chris
Simko, Elemir
Evaluation of inhibition of F4ac positive Escherichia coli attachment with xanthine dehydrogenase, butyrophilin, lactadherin and fatty acid binding protein
title Evaluation of inhibition of F4ac positive Escherichia coli attachment with xanthine dehydrogenase, butyrophilin, lactadherin and fatty acid binding protein
title_full Evaluation of inhibition of F4ac positive Escherichia coli attachment with xanthine dehydrogenase, butyrophilin, lactadherin and fatty acid binding protein
title_fullStr Evaluation of inhibition of F4ac positive Escherichia coli attachment with xanthine dehydrogenase, butyrophilin, lactadherin and fatty acid binding protein
title_full_unstemmed Evaluation of inhibition of F4ac positive Escherichia coli attachment with xanthine dehydrogenase, butyrophilin, lactadherin and fatty acid binding protein
title_short Evaluation of inhibition of F4ac positive Escherichia coli attachment with xanthine dehydrogenase, butyrophilin, lactadherin and fatty acid binding protein
title_sort evaluation of inhibition of f4ac positive escherichia coli attachment with xanthine dehydrogenase, butyrophilin, lactadherin and fatty acid binding protein
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571123/
https://www.ncbi.nlm.nih.gov/pubmed/26374102
http://dx.doi.org/10.1186/s12917-015-0528-0
work_keys_str_mv AT novakovicpredrag evaluationofinhibitionoff4acpositiveescherichiacoliattachmentwithxanthinedehydrogenasebutyrophilinlactadherinandfattyacidbindingprotein
AT charavaryamathchandrashekhar evaluationofinhibitionoff4acpositiveescherichiacoliattachmentwithxanthinedehydrogenasebutyrophilinlactadherinandfattyacidbindingprotein
AT moshynskyyigor evaluationofinhibitionoff4acpositiveescherichiacoliattachmentwithxanthinedehydrogenasebutyrophilinlactadherinandfattyacidbindingprotein
AT lockerbiebetty evaluationofinhibitionoff4acpositiveescherichiacoliattachmentwithxanthinedehydrogenasebutyrophilinlactadherinandfattyacidbindingprotein
AT kaushikradheys evaluationofinhibitionoff4acpositiveescherichiacoliattachmentwithxanthinedehydrogenasebutyrophilinlactadherinandfattyacidbindingprotein
AT loewenmatthewe evaluationofinhibitionoff4acpositiveescherichiacoliattachmentwithxanthinedehydrogenasebutyrophilinlactadherinandfattyacidbindingprotein
AT kidneybeverlya evaluationofinhibitionoff4acpositiveescherichiacoliattachmentwithxanthinedehydrogenasebutyrophilinlactadherinandfattyacidbindingprotein
AT stuartchris evaluationofinhibitionoff4acpositiveescherichiacoliattachmentwithxanthinedehydrogenasebutyrophilinlactadherinandfattyacidbindingprotein
AT simkoelemir evaluationofinhibitionoff4acpositiveescherichiacoliattachmentwithxanthinedehydrogenasebutyrophilinlactadherinandfattyacidbindingprotein