Production of biologically active recombinant ricin B-chain

Tonevitskiĭ, A.G.; Toptygin, A.I.; Agapov, I.I.; Rakhmanova, V.A.; Shamshiev, A.T.; Alekseev, I.O.; Pfueller, U.; Frankel, A.; Tonevitskii, A.G; Toptygin, A.I; Agapov, I.I; Rakhmanova, V.A; Shamshiev, A.T; Alekseev, I.O; Pfueller, U; Frankel, A

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Production of biologically active recombinant ricin B-chain

Tonevitskiĭ, A.G.; Toptygin, A.I.; Agapov, I.I.; Rakhmanova, V.A.; Shamshiev, A.T.; Alekseev, I.O.; Pfueller, U.; Frankel, A.

Molekuliarnaia Biologiia 29(2): 398-406

1995

ISSN/ISBN: 0026-8984

PMID: 7783743

Document Number: 451345

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.