Issue 30, 2020

Structural advances of Siglecs: insight into synthetic glycan ligands for immunomodulation

Abstract

Sialic acid-binding immunoglobulin-like lectins (Siglecs) are transmembrane proteins of the immunoglobulin (Ig) superfamily predominantly expressed on the cells of our immune system. Siglecs recognize sialic acid via their terminal V-set domain. In mammals, sialic acid-terminated glycolipids and glycoproteins are the ligands of Siglecs, and the monomeric affinity of Siglecs for their sialic acid-containing ligands is weak. Significant efforts have been devoted toward the development of chemically modified sialoside ligands to target Siglecs with higher affinity and selectivity. In this review we discuss natural and synthetic sialoside ligands for each human Siglec, emphasizing the ligand binding determinants uncovered from recent advances in protein structural information. Potential therapeutic applications of these ligands are also discussed.

Graphical abstract: Structural advances of Siglecs: insight into synthetic glycan ligands for immunomodulation

Article information

Article type
Review Article
Submitted
30 5 2020
Accepted
09 7 2020
First published
09 7 2020

Org. Biomol. Chem., 2020,18, 5784-5797

Structural advances of Siglecs: insight into synthetic glycan ligands for immunomodulation

L. D. Movsisyan and M. S. Macauley, Org. Biomol. Chem., 2020, 18, 5784 DOI: 10.1039/D0OB01116A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements