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The host transmembrane protein MARCH8, previously known as an expression regulator of host proteins, is a powerful antiviral host factor with a potentially broad antiviral spectrum through two different mechanisms.

Structurally dissimilar N-glycans can be functionally equivalent, and are produced via a self-correcting feature of the Golgi.

Neuronal activity triggers the dispersal of the Golgi into dendritic Golgi satellites, leading to reshaping of the neuronal surface glycoproteome through processing of glycans to mature, sialic acid-containing forms.

A robust procedure to purify mRNAs and their associated proteins identify CFB2 as the critical protein that binds and influences the fate of the main virulence factor in Trypanosoma brucei.

A critical role for glycosylation on viral entry and methods to use this knowledge to reduce SARS-CoV-2 infectivity has been demonstrated.

The transport of proteins along flagellar microtubules generates the force that enables flagella to propel cells across surfaces.

Tick-derived sequence variation in the fusion glycoprotein of Crimean-Congo hemorrhagic fever virus (CCHFV) drastically impairs infection of mammalian cells, suggesting that certain CCHFV strains undergo purifying selection in mammalian hosts.

N-glycans commonly present in the protease domains are required for calnexin-mediated protein folding and intracellular trafficking.

A herpesvirus harnesses the unfolded protein response to regulate its own life cycle, revealing an unexpected role of XBP1u as a potent repressor of the most important viral promoter.

The endoplasmic reticulum (ER) folding sensor UGGT1 essentially cooperates with the peptide editor TAPBPR to provide quality control of MHC I molecules in the antigen presentation pathway.