Glycoconjugates articles from across Nature Portfolio

This protocol details a method for profiling the glycosylation status of antigen-specific antibodies. The protocol consists of an antibody-capture step using an immunosorbent assay similar to enzyme-linked immunosorbent assay, followed by the characterization of captured antibodies using liquid chromatography–mass spectrometry.

O-acetylation is a common modification of sialic acids. Here, a library of synthetic O-acetylated sialosides made it possible to develop an ion mobility mass spectrometry (IM-MS) approach that can elucidate exact O-acetylation patterns and glycosidic linkage types of sialosides isolated from biological samples.

Heparan sulfate (HS) and chondroitin sulfate (CS) are different glycosaminoglycan chains that are attached to core proteins via the same linker tetrasaccharide, and it was unclear how core proteins are specifically modified with HS or CS. Here, the authors determine that the CS-initiating glycosyltransferase CSGALNACT2 is promiscuous, whereas the HS-initiating glycosyltransferase EXTL3 selects only certain core proteins for modification.

The molecular mechanism of syncytium formation during SARS-CoV-2 infection is not fully understood. Zhang et al. now show that cell surface heparan sulfate enhances spike-induced ACE2 clustering and cell-cell fusion, which depends on a conserved ACE2 linker and is blocked by a heparan sulfate binding drug.

Cellular glycosylation is complex and heterogeneous, which is challenging to reproduce synthetically. Here, the authors report on enzymatic remodelling of multivalent glycosylated bacteriophages to produce genetically encoded library of N-glycans which can be used to measure glycan-protein interactions with lectins on the surface of live cells and organs.

Sample preparation and instrumentation for macromolecular mass spectrometry continue to evolve, making the technique more relevant than ever.

As the most abundant class of biomolecules on Earth, carbohydrates are implicated in a multitude of biological functions. Now, a simple chemical transformation has enabled the direct and selective installation of carbohydrates onto a diverse range of small molecules and peptides.

Many nuclear and cytoplasmic proteins are post-translationally modified by both O-GlcNAc and phosphate, but determining whether a single copy of a protein bears multiple modifications remains a challenge. A new analytic approach reveals a surprising correlation between phosphorylation and the O-GlcNAc modification.