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Defining Glycan Recognition by DC-SIGN Using Native Mass Spectrometry
Duong T Bui1, Elena N Kitova1, Lara K Mahal1
1Department of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2, Canada.
ACS Chemical Biology
|July 27, 2026
Summary
Native mass spectrometry reveals dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN) prefers oligomannoses and Lewis antigens. This study defines DC-SIGN
Area of Science:
- Immunology and Glycobiology: Focuses on C-type lectins and their role in immune recognition.
Background:
- C-type lectins (CTLs) are key glycan-binding proteins in immunity.
- Dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN) recognizes diverse glycans but its specificity is unclear.
- Quantifying lectin-glycan affinities is challenging.
Purpose of the Study:
- To characterize the glycan-binding preferences of the DC-SIGN carbohydrate recognition domain (CRD).
- To establish native mass spectrometry (nMS) as a method for profiling CTL-glycan interactions.
Main Methods:
- Utilized native mass spectrometry (nMS), including a catch-and-release (CaR) strategy.
- Employed label- and immobilization-free techniques for quantitative measurements.
- Screened defined libraries of various glycans and examined metal ion binding.
Main Results:
- DC-SIGN CRD showed preference for oligomannoses and Lewis antigens.
- Binding affinity correlated with mannose or fucose residue count.
- Fucosylated N-glycans were identified as DC-SIGN ligands.
- Divalent cations other than Ca2+ had minor effects on ligand binding.
Conclusions:
- Native MS provides a powerful platform for comprehensive CTL interactome profiling.
- Glycan specificity of DC-SIGN was defined, favoring oligomannoses and Lewis antigens.
- This work advances understanding of DC-SIGN's role in immune recognition.
