Modifications of Glycans: Biological Significance and Therapeutic Opportunities

Abstract

Carbohydrates play a central role in a wide range of biological processes. As with nucleic acids and proteins, modifications of specific sites within the glycan chain can modulate a carbohydrate’s overall biological function. For example, acylation, methylation, sulfation, epimerization, and phosphorylation can occur at various positions within a carbohydrate to modulate bioactivity. Therefore, there is significant interest in identifying discrete carbohydrate modifications and understanding their biological effects. Additionally, enzymes that catalyze those modifications and proteins that bind modified glycans provide numerous targets for therapeutic intervention. This review will focus on modifications of glycans that occur after the oligomer/polymer has been assembled, generally referred to as postglycosylational modifications.

Shaping up for structural glycomics: a predictive protocol for oligosaccharide conformational analysis applied to N-linked glycans

“…The molecules and water solvent were modeled using the standard GLYCAM06 26 and TIP3P 41 force fields, respectively. Each carbohydrate was solvated in an explicit water box of equal side length using the Amber12 45 tool tleap, resulting in water boxes of ≈40 Å 3 . Solute atoms were positioned at least 12 Å from the solvent box edge and the assemblies were neutralized, where appropriate, by adding explicit Na + ions.…”

Bacterial polysaccharides as major surface antigens: interest in O-acetyl substitutions

“…It was essentially addressed in relation to sialic acid diversification, thereby underlining its implication in bacterial virulence and disease pathogenesis as well as its ability to alter the host innate and adaptive immunity, and ultimately contribute to bacterial escape. 13,14,19 Many factors, 30 such as the site of O-acetylation or the phase variation O-acetylation profile as in the polysialic acid K1 capsule of E. coli, contribute to this aptitude. subtypes (Fig.…”

Fibulin 2, a Tyrosine O-Sulfated Protein, Is Up-regulated Following Retinal Detachment

“…4C, IB:Myc). Our data suggest that comparable levels of 35 S incorporated in the WT and single mutant clones are due to the fact that Fbln2 is a glycoprotein, and carbohydrates are also sulfated (41). In addition, Fbln2 has been shown to contain four N-linked glycosylation residues at the N-terminal end of the protein (23).…”