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Glycosphingolipids from bovine milk and milk fat globule membranes: a comparative study. Adhesion to enterotoxigenic Escherichia coli strains

  • Fernando Sánchez-Juanes , Josefa M. Alonso , Lorena Zancada and Pablo Hueso
Published/Copyright: October 21, 2008
Biological Chemistry
From the journal Volume 390 Issue 1

Abstract

Several components of milk fat globule membranes (MFGMs) have been reported to display beneficial health properties and some of them have been implicated in the defense of newborns against pathogens. These observations prompted us to determine the glycosphingolipid content of MFGMs and their interaction with pathogens. A comparative study with whole milk components was also carried out. Milk fat globules and MFGMs were isolated from milk. Gangliosides and neutral glycosphingolipids were obtained from MFGMs and whole milk and their fatty acid contents were determined by gas chromatography-mass spectrometry (GC-MS). MFGMs and whole milk showed similar ganglioside and neutral glycosphingolipid contents, with whole milk having more GM3 and glucosylceramide and less GD3, O-acetyl GD3, O-acetyl GT3, and lactosylceramide. The fatty acid content of gangliosides from both sources showed a similar composition. However, the neutral glycosphingolipid fatty acid content seemed to be quite different. Whole milk had fewer very-long-chain fatty acids (18.1% vs. 46.4% in MFGMs) and more medium-chain and unsaturated C18:1 and C18:2 fatty acids. Milk fat globules, MFGMs, lactosylceramide, and gangliosides GM3 and GD3 were observed to bind enterotoxigenic Escherichia coli strains. Furthermore, bacterial hemagglutination was inhibited by MFGMs and glycosphingolipids.

Keywords: bacterial adhesion; fatty acids; gangliosides; newborn defense
Corresponding author
Received: 2008-7-9
Accepted: 2008-9-22
Published Online: 2008-10-21
Published in Print: 2009-01-01

©2009 by Walter de Gruyter Berlin New York

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  2. Editor's Note
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  5. Biochemical characterization of the catalytic domains of three different clostridial collagenases
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  8. Membranes, Lipids, Glycobiology
  9. Glycosphingolipids from bovine milk and milk fat globule membranes: a comparative study. Adhesion to enterotoxigenic Escherichia coli strains
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  12. Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase
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  14. Differential functions of the Apoer2 intracellular domain in selenium uptake and cell signaling
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https://doi.org/10.1515/BC.2009.003
Keywords for this article
bacterial adhesion; fatty acids; gangliosides; newborn defense

Articles in the same Issue

  1. Editor's Note
  2. Editor's Note
  3. Protein Structure and Function
  4. Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence
  5. Biochemical characterization of the catalytic domains of three different clostridial collagenases
  6. Impact of detergents on the activity of acetylcholinesterase and on the effectiveness of its inhibitors
  7. The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein
  8. Membranes, Lipids, Glycobiology
  9. Glycosphingolipids from bovine milk and milk fat globule membranes: a comparative study. Adhesion to enterotoxigenic Escherichia coli strains
  10. Mannose 6-phosphate receptor-dependent endocytosis of lysosomal enzymes is increased in sulfatide-storing kidney cells
  11. Cell Biology and Signaling
  12. Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase
  13. Fibroblast growth factor 2 (FGF-2) is a novel substrate for arginine methylation by PRMT5
  14. Differential functions of the Apoer2 intracellular domain in selenium uptake and cell signaling
  15. Active immunisation against gastric inhibitory polypeptide (GIP) improves blood glucose control in an animal model of obesity-diabetes
  16. Novel Techniques
  17. Applicability of superfolder YFP bimolecular fluorescence complementation in vitro
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