N-glycosylation is normally a cotranslational process that occurs during translocation of the nascent protein to the endoplasmic reticulum. In the present study, however, we demonstrate posttranslational N-glycosylation of recombinant human coagulation factor VII (FVII) in CHO-K1 and 293A cells. Human FVII has two N-glycosylation sites (N145 and N322). Pulse-chase labeled intracellular FVII mig...

background: erythropoietin (epo) is a glycoprotein hormone function to regulate the production of red blood cells. deficiency of epo is known to cause anemia in chronically infected renal patients and they require regular blood transfusion. availability of recombinant epo has eliminated the need for blood transfusion and now it is extensively used for the treatment of anemia. glycosylation of e...

Spondyloarthritis (SpA) is a group of chronic inflammatory arthritic diseases causing back pain and stiffness, leading to irreversible damage joint spine, seriously affecting the quality life. However, exact pathogenesis SpA still unknown, although blockers tumor necrosis factor (TNF) are major therapeutic advance. Of interest association between Immunoglobulin G (IgG) N-glycosylation. IgG N-gl...

background: allergens are mostly composed of glycoprotein structures. it is believed that glycan-specific antibodies may lead to false-positive reactions in immunoassays. in this study we investigated the glycosylation state of grape allergens as well as the presence of antibodies to cross-reactive carbohydrate determinants (anti-ccds) in sera from grape-sensitive individuals. methods: grape ex...

Glycosylation represents the most widespread posttranslational modifications, found in a broad spectrum of natural and therapeutic recombinant proteins. It highly affects bioactivity, site-specificity, stability, solubility, immunogenicity, and serum half-life of glycoproteins. Numerous expression hosts including yeasts, insect cells, transgenic plants, and mammalian cells have been explored fo...

Glycosylation is a ubiquitous modification of lipids and proteins. Despite the essential contribution of glycoconjugates to the viability of all living organisms, diseases of glycosylation in humans have only been identified over the past few decades. The recent development of next-generation DNA sequencing techniques has accelerated the pace of discovery of novel glycosylation defects. The des...

Glycosylation is an important coand post-translational modification involved in a variety of critical biological processes. The development of computational algorithms for protein glycosylation prediction has been propelled in the latest years. The localization of potential glycosylated sites facilitates the rational alteration of glycosylation-related functions in cells. This manuscript gives ...

Three human α-amylases exist: Amy1 (salivary amylase), Amy2A (pancreatic amylase), and Amy2B (expressed in various tissues). These amylases share a 97% 99% amino acid sequence identity, and two potential N-glycosylation sites (N427 and N476) are commonly found in the C-terminal region. In general, salivary amylase is more frequently glycosylated than pancreatic amylase, and it is still uncertai...

Influenza virus typically alters protein glycosylation in order to escape immune pressure from hosts and hence to facilitate survival in different host environments. In this study, the patterns and conservation of glycosylation sites on HA and NA of influenza A/H1N1 viruses isolated from various hosts at different time periods were systematically analyzed, by employing a new strategy combining ...

N-glycosylation is a post-translational modification of proteins that occurs across all three domains life. In Archaea, crucial for cell stability and motility, but importantly also has significant implications virus–host interactions. While some archaeal viruses present glycosylated or interact with host proteins, the direct influence on interactions remains to be elucidated. this study, we ge...