The regulatory power of glycans and their binding partners in immunity

Abstract

Glycans and glycan-binding proteins are central to a properly functioning immune system. Perhaps the best known example of this is the selectin family of surface proteins that are primarily found on leukocytes, and which bind to endothelial glycans near sites of infection or inflammation and enable extravasation into tissues. In the past decade, however, a number of other immune pathways that are dependent on or sensitive to changes in glycan-mediated mechanisms have been revealed. These include antibody function, apoptosis, Th1 versus Th2 skewing, T cell receptor signaling, and MHC class II antigen-presentation. Here, we highlight how regulated changes in protein glycosylation both at the cell surface and on secreted glycoproteins can positively and negatively modulate the immune response.

Contribution of Lewis X Carbohydrate Structure to Neuropathogenic Murine Coronaviral Spread

“…Dynamic immune regulation is induced after interaction between Le x carbohydrate structures and lectins serving as C-type lectin receptors (35), which include scavenger receptor with C-type lectin (SRCL), human dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN), and its mouse homologue SIGN-related-1 (SIGNR1) (36,37). This CRL-mediated signaling can be turned to a pro-(37) or anti-inflammatory status (38,39) depending on the glycan composition or agents that trigger the immune reaction.…”

Glycoproteomic Analysis of Seven Major Allergenic Proteins Reveals Novel Post-translational Modifications

“…APCs are equipped with an array of glycan receptors and targeting such receptors has been shown to induce tolerance (15,(55)(56)(57)(58)(59)(60)(61)(62). The idea that carbohydrates are able to boost and shape the immune response has been tested previously in numerous studies, systematically reviewed in (63). In a food allergy model it has, for example, been shown that oral delivery of bovine serum albumin (BSA) carrying mannoside residues significantly reduce BSA-induced anaphylactic response in the prophylactic setting (64).…”

Recent advances in biosensing using magnetic glyconanoparticles

“…Our group has reported an optimized method for the synthesis of water-soluble magnetic iron oxide nanoparticles using an amphiphilic polymer, poly(maleic anhydride-alt-1-octadecene) [19]. Each anhydride unit yields two carboxylic acid groups on alkaline hydrolysis; this not only results in stabilization of MNPs in water over a broad pH range (4)(5)(6)(7)(8)(9)(10)(11), but also provides a relatively high density of COOH groups for further functionalization. Under standard amide coupling conditions, COOH groups were reacted with NH 2 groups of 4-aminophenyl β-D-glucopyranoside and 4-aminophenyl β-D-galactopyranoside, respectively, to yield the corresponding MNP glyconconjugates (Fig.…”

“…Moreover, correct glycosylation is essential for the folding of proteins and for their biological activity. Abnormal protein glycosylation can be indicative of different diseases, such as cancer and hepatic and autoimmune diseases [3][4][5][6][7]. Consequently, a great deal of research is focused on the development of efficient early diagnostic tools based on glycoprotein detection and identification.…”