Herein, we describe two counterexamples of the previously reported β/α-selectivity 96/4 for glycosylation using ethyl 2-O-[2,3,4-tris-O-tert-butyldimethylsilyl (TBS)-α-L-rhamnopyranosyl]-3,4,6-tris-O-TBS-thio-β-D-glucopyranoside as glycosyl donor. Furthermore, investigated effects protecting group on rhamnose moieties in with cholestanol and revealed that β-selectivity originated from TBS group...

Ensuring consistent glycosylation-associated quality of therapeutic monoclonal antibodies (mAbs) has become a priority in pharmaceutical bioprocessing given that the distribution and composition of the carbohydrates (glycans) bound to these molecules determines their therapeutic efficacy and immunogenicity. However, the interaction between bioprocess conditions, cellular metabolism and the intr...

Background: The information on the role of N-glycosylation is limited. Results: The site and structure of N-glycosylation have evident effects on the activity and stability of CBH. Conclusion: N-glycosylation affects the characteristics of CBHI, and also brings a new function to CBHI as a nonenzymatic synergism factor. Significance: Understanding the effects of N-glycosylation is important for ...

Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST). OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells. Using siRNA to achieve isoform-specific knockdowns, we show that the OST isoforms cooperate and ac...

Among the posttranslational modifications of proteins, glycosylation is probably the most abundant one. Two main types of protein glycosylation have been known for several years, namely N-glycosylation and O-glycosylation. Their biochemical properties, structure and biosynthesis, have been described extensively. Their biological functions are also known for a number of proteins, although in man...

N-linked glycosylation is a post-translational modification that enables the cell to regulate protein function without recourse to the genome. The Proteinase-Activated Receptors (PAR) each possesses a number of N-linked glycosylation sites on their extracellular domains. However, little is currently known about the relative glycosylation status of each family member and about the influence that...

Antigenic drift in the influenza A virus hemagglutinin (HA) is responsible for seasonal reformulation of influenza vaccines. Here, we address an important and largely overlooked issue in antigenic drift: how does the number and location of glycosylation sites affect HA evolution in man? We analyzed the glycosylation status of all full-length H1 subtype HA sequences available in the NCBI influen...

Cellular glycosylation processes are vital to cell functioning. In malignant cells, they are profoundly altered. We used time-course gene expression data from the NCI-60 cancer cell lines treated with 11 antitumor agents to analyze expression changes of genes involved in glycosylation pathways, genes encoding glycosylation targets or regulators, and members of cancer pathways affected by glycos...

Changes in protein glycosylation are related to different diseases and have a potential as diagnostic and prognostic disease biomarkers. Transferrin (Tf) glycosylation changes are common marker for congenital disorders of glycosylation. However, biological interindividual variability of Tf N-glycosylation and genes involved in glycosylation regulation are not known. Therefore, high-throughput T...

Over 100 human genetic disorders result from mutations in glycosylation-related genes. In 2013, a new glycosylation disorder was reported every 17 days. This trend will probably continue given that at least 2% of the human genome encodes glycan-biosynthesis and -recognition proteins. Established biosynthetic pathways provide many candidate genes, but finding unanticipated mutated genes will off...