Identification of escherichia coli F4ac-binding proteins in porcine milk fat globule membrane

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TypeArticle
Journal titleCanadian Journal of Veterinary Research
ISSN0830-9000
Volume79
Issue2
Pages120128; # of pages: 9
Subjectadipophilin; binding protein; butyrophilin; fatty acid binding protein 3; lactadherin; long chain fatty acid coenzyme A ligase 3; membrane protein; affinity chromatography; binding affinity; enterotoxigenic Escherichia coli; F4ac fimbria; fimbria; liquid chromatography; mass spectrometry; membrane; milk fat globule membrane; nonhuman; polyacrylamide gel electrophoresis; protein analysis; swine; Western blotting; Bacteria (microorganisms); Escherichia coli; Sus
AbstractF4ac-positive enterotoxigenic Escherichia coli (ETEC) must attach to the intestinal mucosa to cause diarrhea in piglets. Prevention of bacterial attachment to the intestinal mucosa is the most effective defense against ETEC-induced diarrhea. Porcine milk fat globule membranes (MFGM) were shown to be able to inhibit attachment of ETEC to the intestinal brush border; however, the specific components of porcine MFGM that inhibited attachment of ETEC to enterocytes were not identified. Accordingly, the purpose of this study was to identify F4ac-binding MFGM proteins by overlay Western blot and affinity chromatography. The proteome of porcine MFGM was characterized and the following F4ac-binding proteins were detected by overlay Western blot and affinity chromatography: lactadherin, butyrophilin, adipophilin, acyl-CoA synthetase 3, and fatty acid-binding protein 3. The biological function of these proteins was not investigated but it is possible that their interaction with F4ac fimbria interferes with bacterial attachment and colonization.
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PublisherNational Centre for Biotechnology Information
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); Human Health Therapeutics
Peer reviewedYes
NPARC number21275759
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Record identifier20791c78-da6d-45fa-9039-9ab172168d68
Record created2015-07-14
Record modified2016-05-09
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