Glycosylation articles from across Nature Portfolio

NGLY1 mutations cause a multisystem developmental disorder. Here they show that this enzyme is required for normal gut barrier function, and when mutated, causes immune and metabolic abnormalities, contributing to lethality.

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.

Glycoproteomics is coming of age, thanks to advances in instrumentation, experimental methodologies and computational search algorithms.

A two-step chemoenzymatic method for N-glycan subtype-selective editing.

Influenza vaccine strain selection is informed by international efforts to track antigenic change, focusing on the viral hemagglutinin protein. Recent research advocates monitoring neuraminidase for immune escape mutations that could reduce vaccine efficacy.