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

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	398-406
Number of pages	9
Journal	Molekulyarnaya Biologiya
Volume	29
Issue number	2
State	Published - 1995

ASJC Scopus subject areas

General Medicine

Cite this

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title = "Recombinant ricin B chain produced in Escherichia coli is biologically active",

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.",

author = "Tonevitsky, {A. G.} and {Toptygin Yu.}, A. and Agapov, {I. I.} and Rakhmanova, {V. A.} and Shamshiev, {A. T.} and {Alekseev Yu.}, O. and U. Pfuller and A. Frankel",

year = "1995",

language = "English (US)",

volume = "29",

pages = "398--406",

journal = "Molekulyarnaya Biologiya",

issn = "0026-8984",

publisher = "Russian Academy of Sciences",

number = "2",

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TY - JOUR

T1 - Recombinant ricin B chain produced in Escherichia coli is biologically active

AU - Tonevitsky, A. G.

AU - Toptygin Yu., A.

AU - Agapov, I. I.

AU - Rakhmanova, V. A.

AU - Shamshiev, A. T.

AU - Alekseev Yu., O.

AU - Pfuller, U.

AU - Frankel, A.

PY - 1995

Y1 - 1995

N2 - 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.

AB - 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.

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M3 - Article

C2 - 7783743

AN - SCOPUS:0029264489

SN - 0026-8984

VL - 29

SP - 398

EP - 406

JO - Molekulyarnaya Biologiya

JF - Molekulyarnaya Biologiya

IS - 2

ER -

Recombinant ricin B chain produced in Escherichia coli is biologically active

Abstract

ASJC Scopus subject areas

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