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Probing the pH-dependency of DC-SIGN/R multivalent lectin-glycan interactions using polyvalent glycan-gold

Rahman Basaran¹, Xinyu Ning¹, Darshita Budhadev¹

¹School of Chemistry, Astbury Centre for Structural Molecular Biology, University of Leeds Leeds LS2 9JT UK d.zhou@leeds.ac.uk.

Nanoscale Advances

|April 18, 2024

Summary

Dendritic cell lectin (DC-SIGN) and DC-SIGNR exhibit distinct pH-dependent binding to viral ligands. Understanding this pH sensitivity is crucial for viral transmission research.

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Area of Science:

Molecular Biology
Immunology
Virology

Background:

Dendritic cell-specific intercellular factor (DC-SIGN) and its homolog DC-SIGNR are key lectins involved in viral binding and transmission.
These lectins mediate the uptake and release of viruses like Ebola, HIV, HCV, and SARS-CoV-2 through intracellular trafficking pathways.
The pH-dependent binding properties of DC-SIGN/R with glycan ligands are critical for understanding viral transmission mechanisms.

Purpose of the Study:

To investigate the pH-dependent multivalent lectin-glycan interaction (MLGI) properties of DC-SIGN and DC-SIGNR.
To utilize novel glycosylated gold nanoparticle (glycan-GNP) probes for quantitative analysis of DC-SIGN/R MLGI.
To elucidate the structural information, binding site orientation, and binding modes of DC-SIGN/R under varying pH conditions.

Main Methods:

Development of densely glycosylated gold nanoparticles (glycan-GNPs) as probes for DC-SIGN/R MLGI.
Quantitative measurement of MLGI affinities and structural information using glycan-GNP probes.
Investigation of pH dependency of DC-SIGN/R MLGI across a physiological to lysosomal pH range (7.4 to ~4.6).

Main Results:

DC-SIGN exhibits strong and stable binding to glycan-GNPs from pH 7.4 to ~5.8, with significantly weakened binding at pH ≤ 5.4 and potential dissociation at pH 4.6.
DC-SIGNR shows enhanced affinity for glycan-GNPs as pH decreases from 7.4 to 5.4, with optimal binding at pH 5.4, followed by reduced affinity at lower pH.
Both DC-SIGN and DC-SIGNR binding with glycan-GNPs demonstrate partial reversibility in a pH-dependent manner.

Conclusions:

DC-SIGN/R's distinct pH-dependent binding properties are crucial for their roles in viral interactions and intracellular trafficking.
The observed pH-dependent behavior of DC-SIGN aligns with its function as an endocytic recycling receptor.
Glycan-GNP probes are effective tools for studying the complex, pH-sensitive mechanisms of DC-SIGN/R multivalent lectin-glycan interactions.