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Expression of single-chain antibody-barstar fusion in plants.
- Source :
-
Biochimie [Biochimie] 2007 Jan; Vol. 89 (1), pp. 31-8. Date of Electronic Publication: 2006 Aug 10. - Publication Year :
- 2007
-
Abstract
- We successfully cloned and expressed a single-chain antibody (425scFv), that is directed to human epidermal growth factor receptor HER1 (EGFR) in transgenic tobacco plants as a fusion with bacterial barstar gene (425scFv-barstar). Plant-produced recombinant 425scFv-barstar was recovered using barstar-barnase system. Based on barstar-barnase affinity, during purification of the plant-produced 425scFv-barstar, we generated bispecific scFv-antibody heterodimers from individual single-chain fragments initially produced in different host systems with binding activity to both HER1 and HER2/neu tumor antigens. We demonstrated by flow cytometry and indirect immunofluorescent microscopy that both the components of heterodimer retain its specific cell-binding activity.
- Subjects :
- Bacterial Proteins genetics
Blotting, Western
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Enzyme-Linked Immunosorbent Assay
Flow Cytometry
Humans
Immunoglobulin Fragments immunology
Microscopy, Fluorescence
Plants, Genetically Modified
Receptor, ErbB-2
Recombinant Fusion Proteins immunology
ErbB Receptors immunology
Immunoglobulin Fragments biosynthesis
Protein Engineering methods
Recombinant Fusion Proteins biosynthesis
Nicotiana genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0300-9084
- Volume :
- 89
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochimie
- Publication Type :
- Academic Journal
- Accession number :
- 16938381
- Full Text :
- https://doi.org/10.1016/j.biochi.2006.07.012