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Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Increasing the Chemical Space of L-SIGN Specific Glycomimetics.

Gianluca Cavazzoli¹, Clara Delaunay², Sara Pollastri¹

¹Dipartimento di Chimica, Università degli Studi di Milano, via Golgi 19, Milano 20133, Italy.

Journal of Medicinal Chemistry

|October 18, 2025

Summary

This summary is machine-generated.

Researchers developed new mannose glycomimetics that bind to L-SIGN, a C-type lectin receptor. These compounds show high selectivity for L-SIGN, matching or improving upon previous versions for potential antiviral therapies.

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Area of Science:

Biochemistry
Structural Biology
Drug Discovery

Background:

C-type lectin receptors like L-SIGN are targets for antiviral therapies and drug delivery.
Previous work identified Man84 as a selective L-SIGN ligand with micromolar affinity.
High selectivity against homologue lectins, such as DC-SIGN, is crucial.

Purpose of the Study:

To design and synthesize novel Man84 isosteres (ligands 2-11) with maintained or improved L-SIGN selectivity.
To evaluate the binding affinity and selectivity of these new ligands against L-SIGN and DC-SIGN.
To elucidate the structural basis of ligand binding to L-SIGN.

Main Methods:

Synthesis of Man84 isosteres (ligands 2-11).
Surface Plasmon Resonance (SPR) inhibition assays using immobilized SARS-CoV-2 Spike protein to measure L-SIGN and DC-SIGN binding affinity and selectivity.
X-ray crystallography to determine the structure of the L-SIGN CRD/ligand 4 complex.

Main Results:

Compounds 4, 5, and 9 demonstrated low micromolar affinity for L-SIGN.
These compounds exhibited 50-94 fold selectivity for L-SIGN over DC-SIGN, matching or surpassing Man84.
The crystal structure revealed a key bidentate hydrogen bond interaction between ligand 4 and L-SIGN residue E370.

Conclusions:

The developed Man84 isosteres represent potent and selective L-SIGN ligands.
These findings support the potential of these compounds in antiviral strategies and targeted delivery systems.
Structural insights provide a basis for further optimization of L-SIGN targeting ligands.