ArticleMolecular & cellular proteomics : MCP2012
Glycosylation of human milk lactoferrin exhibits dynamic changes during early lactation enhancing its role in pathogenic bacteria-host interactions.
Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT01817127 (Functional Deconstruction of Human Milk Oligosaccharides and Lipids), which is not on this map. Cited by 63 papers, 2 of them syntheses that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Functional Deconstruction of Human Milk Oligosaccharides and Lipids
Who cites it
63 citing papers in PubMed, 2 syntheses or guidelines pooled it, 173 citations in OpenAlex.
- Enteral lactoferrin supplementation for prevention of sepsis and necrotizing enterocolitis in preterm infants.The Cochrane database of systematic reviews · 2020Pooled it
- Enteral lactoferrin supplementation for prevention of sepsis and necrotizing enterocolitis in preterm infants.The Cochrane database of systematic reviews · 2017Pooled it
- Sequence-Based and Functional Analysis for the Discovery of N-Glycan Degrading Glycosidases From the Microbial Metagenome of the Infant Gut.MicrobiologyOpen · 2026Article
- Proteomic andMicrobiology spectrum · 2025Article
- Microbial community of civet excreta fed by robusta cherry coffee in Indonesian civet coffee production.Journal of advanced veterinary and animal research · 2025Article
- Identification and comparison ofFood chemistry: X · 2025Article
- The ferroform and glycoform landscape of human milk lactoferrin dissected through hybrid mass spectrometric approaches.Frontiers in nutrition · 2025Article
- Characterization of recombinant human lactoferrin expressed inThe Analyst · 2024Article
- Lactoferrins in Their Interactions with Molecular Targets: A Structure-Based Overview.Pharmaceuticals (Basel, Switzerland) · 2024Review
- The Yin and Yang of pathogens and probiotics: interplay betweenFrontiers in microbiology · 2024Article
- The Multifaceted Roles of Bovine Lactoferrin: Molecular Structure, Isolation Methods, Analytical Characteristics, and Biological Properties.Journal of agricultural and food chemistry · 2023Review
- Time to Kill and Time to Heal: The Multifaceted Role of Lactoferrin and Lactoferricin in Host Defense.Pharmaceutics · 2023Review
- Changes in glycosylated proteins in colostrum and mature milk and their implication.Frontiers in nutrition · 2023Article
- Lactoferrin Decreases EnterotoxigenicPharmaceutics · 2022Article
- Lactoferrin as a Human Genome "Guardian"-An Overall Point of View.International journal of molecular sciences · 2022Review
- Shiga Toxin-ProducingMicroorganisms · 2022Review
- Immobilization of a Bifidobacterial Endo-Frontiers in bioengineering and biotechnology · 2022Article
- A Novel Human Recombinant Lactoferrin Inhibits Lung Adenocarcinoma Cell Growth and Migration with No Cytotoxic Effect on Normal Human Epithelial Cells.Archivum immunologiae et therapiae experimentalis · 2021Article
- Diverse Mechanisms of Antimicrobial Activities of Lactoferrins, Lactoferricins, and Other Lactoferrin-Derived Peptides.International journal of molecular sciences · 2021Review
- Comprehensive structural glycomic characterization of the glycocalyxes of cells and tissues.Nature protocols · 2020Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 2 institutions in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.