Evidence map›Paper›PMID 26976925›Full record

ArticleThe Biochemical journal2016

Human DC-SIGN binds specific human milk glycans.

Alexander J Noll, Ying Yu, Yi Lasanajak, Geralyn Duska-McEwen, Rachael H Buck, David F Smith, Richard D Cummings

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
7.2field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

45 citing papers in PubMed, 87 citations in OpenAlex.

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  18. Biology of human milk oligosaccharides: From basic science to clinical evidence.Journal of human nutrition and dietetics : the official journal of the British Dietetic Association · 2022
    Review
  19. Review
  20. Role of milk carbohydrates in intestinal health of nursery pigs: a review.Journal of animal science and biotechnology · 2022
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Alexander J NollThe Glycomics Center, Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, U.S.A. Program in Microbiology and Molecular Genetics, Graduate Division of Biological and Biomedical Sciences, Laney Graduate School, Emory University, Atlanta, GA 30322, U.S.A.
Ying YuThe Glycomics Center, Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, U.S.A.
Yi LasanajakThe Glycomics Center, Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, U.S.A.
Geralyn Duska-McEwenAbbott Nutrition, Global Discovery R&D, Columbus, OH 43215, U.S.A.
Rachael H BuckAbbott Nutrition, Global Discovery R&D, Columbus, OH 43215, U.S.A.
David F SmithThe Glycomics Center, Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, U.S.A.
Richard D CummingsThe Glycomics Center, Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, U.S.A. rcummin1@bidmc.harvard.edu.
Emory University · USDiscovery Laboratories (United States) · US

Funding

Overall Priority Score P41GM103694 · NIGMS · EMORY UNIVERSITY · PI CUMMINGS, RICHARD D · 2013 to 2018
$6.9M
NIGMS NIH HHS P41 GM103694
6 · The paper itself

Abstract

Human milk glycans (HMGs) are prebiotics, pathogen receptor decoys and regulators of host physiology and immune responses. Mechanistically, human lectins (glycan-binding proteins, hGBP) expressed by dendritic cells (DCs) are of major interest, as these cells directly contact HMGs. To explore such interactions, we screened many C-type lectins and sialic acid-binding immunoglobulin-like lectins (Siglecs) expressed by DCs for glycan binding on microarrays presenting over 200 HMGs. Unexpectedly, DC-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) showed robust binding to many HMGs, whereas other C-type lectins failed to bind, and Siglec-5 and Siglec-9 showed weak binding to a few glycans. By contrast, most hGBP bound to multiple glycans on other microarrays lacking HMGs. An α-linked fucose residue was characteristic of HMGs bound by DC-SIGN. Binding of DC-SIGN to the simple HMGs 2'-fucosyl-lactose (2'-FL) and 3-fucosyl-lactose (3-FL) was confirmed by flow cytometry to beads conjugated with 2'-FL or 3-FL, as well as the ability of the free glycans to inhibit DC-SIGN binding. 2'-FL had an IC50 of ∼1 mM for DC-SIGN, which is within the physiological concentration of 2'-FL in human milk. These results demonstrate that DC-SIGN among the many hGBP expressed by DCs binds to α-fucosylated HMGs, and suggest that such interactions may be important in influencing immune responses in the developing infant.

Indexed as

Cell Adhesion MoleculesDC-Specific ICAM-3 Grabbing NonintegrinDendritic CellsHumansLectins, C-TypeMilk, HumanPolysaccharidesProtein Array AnalysisProtein BindingReceptors, Cell SurfaceSialic Acid Binding Immunoglobulin-like LectinsTrisaccharides2'-fucosyllactoseCell Adhesion MoleculesDC-Specific ICAM-3 Grabbing NonintegrinLectins, C-TypePolysaccharidesReceptors, Cell SurfaceSialic Acid Binding Immunoglobulin-like LectinsTrisaccharidesdendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN)glycan-binding proteinsglycan microarraysglycan recognitionhuman milk glycanslectins

Identifiers

PMID26976925
PMCPMC4875834
OpenAlexW2300446299

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.