Plant species and organ influence the structure and subcellular localization of recombinant glycoproteins
Autor: | Johannes Stadlmann, Sylvain Marcel, Eva Stoger, Thomas W. Rademacher, Markus Sack, Friedrich Altmann, Elsa Arcalis |
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Přispěvatelé: | Publica |
Rok vydání: | 2013 |
Předmět: |
Glycosylation
Arabidopsis Plant Science HIV Antibodies law.invention Fungal Proteins Species Specificity Polysaccharides law Tobacco Genetics Glycoproteins chemistry.chemical_classification 6-Phytase Production area Downstream processing biology Protein Stability Antibodies Monoclonal General Medicine Plants Genetically Modified Subcellular localization biology.organism_classification Recombinant Proteins Cell biology Plant Leaves Protein Transport chemistry Biochemistry Seeds Plant species Recombinant DNA Aspergillus niger Glycoprotein Agronomy and Crop Science Broadly Neutralizing Antibodies Protein trafficking |
Zdroj: | Plant Molecular Biology. 83:105-117 |
ISSN: | 1573-5028 0167-4412 |
Popis: | Many plant-based systems have been developed as bioreactors to produce recombinant proteins. The choice of system for large-scale production depends on its intrinsic expression efficiency and its propensity for scale-up, post-harvest storage and downstream processing. Factors that must be considered include the anticipated production scale, the value and intended use of the product, the geographical production area, the proximity of processing facilities, intellectual property, safety and economics. It is also necessary to consider whether different species and organs affect the subcellular trafficking, structure and qualitative properties of recombinant proteins. In this article we discuss the subcellular localization and N-glycosylation of two commercially-relevant recombinant glycoproteins (Aspergillus niger phytase and anti-HIV antibody 2G12) produced in different plant species and organs. We augment existing data with novel results based on the expression of the sa me recombinant proteins in Arabidopsis and tobacco seeds, focusing on similarities and subtle differences in N-glycosylation that often reflect the subcellular trafficking route and final destination, as well as differences generated by unique enzyme activities in different species and tissues. We discuss the potential consequences of such modifications on the stability and activity of the recombinant glycoproteins. |
Databáze: | OpenAIRE |
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