NDLI: Glycosylation of human milk lactoferrin exhibits dynamic changes during early lactation enhancing its role in pathogenic bacteria-host interactions.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Barboza, Mariana Pinzon, Janneth Wickramasinghe, Saumya Froehlich, John W. Moeller, Isabelle Smilowitz, Jennifer T. Ruhaak, L. Renee Huang, Jincui Lönnerdal, Bo German, J. Bruce Medrano, Juan F. Weimer, Bart C. Lebrilla, Carlito B.
Description	Country affiliation: United States Author Affiliation: Barboza M ( Department of Chemistry, Functional Glycobiology Program, University of California Davis. One Shields Ave, Davis, California 95616, USA.)
Abstract	Human milk lactoferrin (hmLF) is the most abundant glycoprotein present in human milk and displays a broad range of protective functions in the gut of newborn infants. hmLF is N-glycosylated, but little is known about the lactation stage-related development of the glycosylation phenotype. hmLF glycosylation from milk samples from five donors during the first 10 weeks of lactation was assessed and observed to be more diverse than previously reported. During this period dynamic changes in glycosylation were observed corresponding to a decrease in glycosylation in the second week followed by an increase in total glycosylation as well as higher order fucosylation thereafter. Gene expression analysis was performed in milk somatic cells from a sixth subject. It was found that fucosyltransferase expression increased during entire period, whereas expression of genes for the oligosaccharyl transferase complex decreased in the second week. The effect of hmLF glycosylation was examined for the protein's ability to affect bacterial binding to epithelial cells. hmLF significantly inhibited pathogen adhesion and purified hmLF glycans significantly reduced Salmonella invasion of colonic epithelial cells to levels associated with non-invasive deletion mutants. This study indicates that hmLF glycosylation is tightly regulated by gene expression and that glyco-variation is involved in modulating pathogen association.
File Format	HTM / HTML
ISSN	15359476
e-ISSN	15359484
DOI	10.1074/mcp.M111.015248
Journal	Molecular & Cellular Proteomics
Issue Number	6
Volume Number	11
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2012-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Proteomics Host-pathogen Interactions Lactation Lactoferrin Metabolism Milk, Human Protein Processing, Post-translational Bacterial Adhesion Carbohydrate Conformation Carbohydrate Sequence Cell Line Escherichia Coli O157 Physiology Fourier Analysis Fucosyltransferases Genetics Gene Expression Profiling Gene Expression Regulation Glycosylation Hexosyltransferases Membrane Proteins Polysaccharides Chemistry Salmonella Sequence Analysis, Rna Spectrometry, Mass, Matrix-assisted Laser Desorption-ionization Research Support, N.i.h., Extramural
Content Type	Text
Resource Type	Article
Subject	Medicine Analytical Chemistry Molecular Biology Biochemistry

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Glycosylation of Human Milk Lactoferrin Exhibits Dynamic Changes During Early Lactation Enhancing Its Role in Pathogenic Bacteria-Host Interactions*

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Glycosylation of Human Milk Lactoferrin Exhibits Dynamic Changes During Early Lactation Enhancing Its Role in Pathogenic Bacteria-Host Interactions*

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