Recombinant ricin B chain produced in Escherichia coli is biologically active

A. G. Tonevitsky, A. Toptygin Yu., I. I. Agapov, V. A. Rakhmanova, A. T. Shamshiev, O. Alekseev Yu., U. Pfuller, A. Frankel

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Abstract

Escherichia coli cells transformed with plasmids containing ricin B-chain coding sequences are shown to express this heterologous protein in inclusion bodies. After denaturation and renaturation of the product in the presence of glutathione and lactose, the recombinant ricin B-chain is soluble, biologically active and stable. Cytotoxicity of heterodimer containing this protein and ricin A-chain is found to be only ten times lower than that of native ricin. Recombinant B-chain alone was nontoxic to cells (ID50 > 10-6 M). Our data suggest that ricin B-chain oligosaccharides are essential for stability preserving protein from proteolytic degradation in cells.

Original languageEnglish (US)
Pages (from-to)398-406
Number of pages9
JournalMolekulyarnaya Biologiya
Volume29
Issue number2
Publication statusPublished - 1995

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ASJC Scopus subject areas

  • Molecular Biology

Cite this

Tonevitsky, A. G., Toptygin Yu., A., Agapov, I. I., Rakhmanova, V. A., Shamshiev, A. T., Alekseev Yu., O., ... Frankel, A. (1995). Recombinant ricin B chain produced in Escherichia coli is biologically active. Molekulyarnaya Biologiya, 29(2), 398-406.