Construction and analysis of a novel peptide tag containing an unnatural N-glycosylation site
| Autor: | Astrid Lusch, Markus Berger, Johanna Dörsing, Rudolf Tauber, Vera Vivian Saul, Matthias Kaup, Véronique Blanchard |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Signal peptide
Glycosylation Stereochemistry Molecular Sequence Data Biophysics Sequence (biology) Peptide CHO Cells Biology Biochemistry chemistry.chemical_compound Cricetulus Polysaccharides Structural Biology Cricetinae Genetics Animals Humans Amino Acid Sequence N-Glycosylation Site Molecular Biology Peptide sequence chemistry.chemical_classification GlycoTag Chinese hamster ovary cell Glycopeptides Cell Biology Alpha-1 antitrypsin Amino acid carbohydrates (lipids) HEK293 Cells chemistry alpha 1-Antitrypsin Peptides |
| Zdroj: | FEBS Letters. 585:2372-2376 |
| ISSN: | 0014-5793 |
| Popis: | The addition of N-glycans to clinically used proteins enhances their therapeutic features. Here we report the design of a novel peptide tag with an unnatural N-glycosylation site, which may increase the N-glycan content of generally any protein. The designed GlycoTags were attached to A1AT, EPO and AGP and constructs were expressed in HEK293 or CHO cells. Hereby we could prove that the attached unnatural N-glycosylation site is decorated with complex-type N-glycans and that the spacer as well as the C-terminal “tail” sequence are critical for the usage of the novel N-glycosylation site. This demonstrates that the novel GlycoTag is a convenient tool to provide proteins with extra N-glycan moieties by simply adding a peptide tag sequence as small as 22 amino acids. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text