Protein N-glycosylation is a metabolic process that has been highly conserved in evolution. In all eukaryotes, N-glycosylation is obligatory for viability. It functions by modifying appropriate asparagine residues of proteins with oligosaccharide structures, thus influencing their properties and bioactivities. N-glycoprotein biosynthesis involves a multitude of enzymes, glycosyltransferases, an...

context advanced glycation end-products (ages) are signaling proteins associated to several vascular and neurological complications in diabetic and non-diabetic patients. ages proved to be a marker of negative outcome in both diabetes management and surgical procedures in these patients. the reported role of ages prompted the development of pharmacological inhibitors of their effects, giving ri...

The analysis of HIV-1 envelope carbohydrates is critical to understanding their roles in HIV-1 transmission as well as in binding of envelope to HIV-1 antibodies. However, direct analysis of protein glycosylation by glycopeptide-based mass mapping approaches involves structural simplification of proteins with the use of a protease followed by an isolation and/or enrichment step before mass anal...

Serine-rich repeat glycoproteins (SRRPs) are conserved in Gram-positive bacteria. They are crucial for modulating biofilm formation and bacterial-host interactions. Glycosylation of SRRPs plays a pivotal role in the process; thus understanding the glycosyltransferases involved is key to identifying new therapeutic drug targets. The glycosylation of Fap1, an SRRP of Streptococcus parasanguinis, ...

BACKGROUND Inherited deficiency of phosophomannomutase (PMM2) causes a human glycosylation disorder known as Congenital Disorder of Glycosylation Ia. CASE PRESENTATION Herein, we describe a case of congenital disorder of glycosylation Ia, presented with recurrent pericardial effusion and unusual findings of inverted nipples, fat pads, reduced deep-tendon reflexes and multisystem involvement. ...

This tutorial is planned for biologists and computational biologists interested in bioinformatics applications to study protein glycosylation. Glycosylation is a coand post-translational modification that involves the selective attachment of carbohydrates to proteins. The enhancement of glycosylation by applying glycoengineering strategies has become widely used to improve properties for protei...

Intravenous immunoglobulin (IVIg) products from different pharmaceutical companies vary in composition, in part because of the selected blood donors and production process. N-glycosylation of the Fc-portion of IgG varies between blood donors and may influence both the side-effects and therapeutic effectiveness of IVIg. At present, the variation in Fc N-glycosylation between IVIg products has no...