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

Research output: Contribution to journalArticle

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
StatePublished - 1995

ASJC Scopus subject areas

  • Medicine(all)

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