Expression of single-chain antibody-barstar fusion in plants

Ekaterina G. Semenyuk, Oleg A. Stremovskiy, Evelina F. Edelweiss, Olga V. Shirshikova, Taras G. Balandin, Yaroslav I. Buryanov, Sergey M. Deyev

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26 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)31-38
Number of pages8
JournalBiochimie
Volume89
Issue number1
DOIs
Publication statusPublished - Jan 2007
Externally publishedYes

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Keywords

  • Barnase
  • Barstar
  • HER1 (EGFR)
  • Single-chain Fv antibody
  • Transgenic plants

ASJC Scopus subject areas

  • Biochemistry

Cite this

Semenyuk, E. G., Stremovskiy, O. A., Edelweiss, E. F., Shirshikova, O. V., Balandin, T. G., Buryanov, Y. I., & Deyev, S. M. (2007). Expression of single-chain antibody-barstar fusion in plants. Biochimie, 89(1), 31-38. https://doi.org/10.1016/j.biochi.2006.07.012