| Literature DB >> 16938381 |
Ekaterina G Semenyuk1, Oleg A Stremovskiy, Evelina F Edelweiss, Olga V Shirshikova, Taras G Balandin, Yaroslav I Buryanov, Sergey M Deyev.
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.Entities:
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Year: 2006 PMID： 16938381 DOI： 10.1016/j.biochi.2006.07.012
Source DB: PubMed Journal: Biochimie ISSN： 0300-9084 Impact factor: 4.079