Humanizing glycosylation pathways in eukaryotic expression systems

Humanizing glycosylation pathways in eukaryotic expression systems.

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...

Investigating Asparagine-Linked Protein Glycosylation in Eukaryotic and Prokaryotic Systems

Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems.

Asparagine-linked protein glycosylation is a prevalent protein modification reaction in eukaryotic systems. This process involves the co-translational transfer of a pre-assembled tetradecasaccharide from a dolichyl-pyrophosphate donor to the asparagine side chain of nascent proteins at the endoplasmic reticulum (ER) membrane. Recently, the first such system of N-linked glycosylation was discove...

Expression of Influenza Heamagglutinin Globular Head in Different Eukaryotic Cells

Background and Aims: Influenza (flu) is a respiratory infection in mammals and birds. It is caused by an RNA virus in the family Orthomyxoviridae. The virus is divided into three main types. Influenza virus type A is found in a wide variety of bird and mammal species and can undergo major shifts in immunological properties. Hemagglutinin (HA) is an important influenza virus surface antigen that...

Protein glycosylation pathways in filamentous fungi.

Glycosylation of proteins is important for protein stability, secretion, and localization. In this study, we have investigated the glycan synthesis pathways of 12 filamentous fungi including those of medical/agricultural/industrial importance for which genomes have been recently sequenced. We have adopted a systems biology approach to combine the results from comparative genomics techniques wit...