Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Proteoglycans

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

A Retrospective Review of Drug-Induced Sleep Endoscopy Evaluating Upper Airway Dynamics in Patients with Vagus Nerve Stimulator-Induced Obstructive Sleep Apnea.

Clinical and experimental otorhinolaryngology·2026

Same author

Modeling 24-Hour Blood Pressure Rhythms Using Mixed-Effects Cosinor Models.

Journal of biological rhythms·2026

Same author

Advanced Imaging to Assess Airway Dynamics.

Otolaryngologic clinics of North America·2026

Same author

Selective antimicrobial potential of fucoidans against the pathogen <i>Listeria monocytogenes</i>.

Frontiers in microbiology·2026

Same author

A unique blend of five human milk oligosaccharides supports recovery of infant microbiome composition and function after <i>ex vivo</i> antibiotic use.

Frontiers in pediatrics·2026

Same author

Long-Term Associations of Early-Life Human Milk Oligosaccharide Intake with Allergic Disease Development and Gut Microbiota Profiles in 5-Year-Old Children.

Nutrients·2026

Search research articles

Related Experiment Video

Updated: Mar 24, 2026

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Published on: April 13, 2019

Human DC-SIGN binds specific human milk glycans.

Alexander J Noll¹, Ying Yu², Yi Lasanajak²

¹The 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.

The Biochemical Journal

|March 16, 2016

Summary

Human milk glycans (HMGs) bind to DC-SIGN, a lectin on dendritic cells (DCs). This interaction, particularly with α-fucosylated HMGs like 2'-fucosyl-lactose (2'-FL), may influence infant immune responses.

Keywords:

dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN)glycan microarrays glycan recognition glycan-binding proteins human milk glycans lectins

More Related Videos

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples

Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples

Published on: May 4, 2012

Related Experiment Videos

Last Updated: Mar 24, 2026

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Published on: April 13, 2019

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples

Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples

Published on: May 4, 2012

Area of Science:

Immunology
Glycobiology
Human milk oligosaccharides

Background:

Human milk glycans (HMGs) are crucial for infant health, acting as prebiotics and immune modulators.
Dendritic cells (DCs) express human glycan-binding proteins (hGBPs) that interact with HMGs, influencing immune responses.

Purpose of the Study:

To investigate the binding interactions between various hGBPs on DCs and a wide array of HMGs.
To identify specific hGBPs and HMG structures involved in these interactions.

Main Methods:

Screening of C-type lectins and Siglecs on DCs for HMG binding using microarrays.
Validation of DC-SIGN binding to specific HMGs (2 -FL, 3-FL) via flow cytometry.
Determination of 2 -FL binding affinity to DC-SIGN.

Main Results:

DC-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) exhibited strong binding to numerous HMGs, unlike other tested lectins.
α-linked fucose residues characterized HMGs preferentially bound by DC-SIGN.
DC-SIGN demonstrated specific binding to 2 -fucosyl-lactose (2 -FL) and 3-fucosyl-lactose (3-FL) at physiologically relevant concentrations.

Conclusions:

DC-SIGN is a key hGBP on DCs that binds α-fucosylated HMGs.
These interactions suggest a role for DC-SIGN in mediating the immunomodulatory effects of HMGs in infants.