Comparison of properties of mistletoe lectin I A‐chain and ricin B‐Chain conjugate with native toxins

FEBS Letters

Tonevitsky, A.G.¹  Agapov, I.I.¹  Pfuller, K.²  Toptygin, A.Yu.³  Ershova, E.V.¹  Shamshiev, A.T.¹  Pfuller, U.² 

[1] Institute for Genetics of Microorganisms, 1-st Dorozhny Proezd 1, Moscow 113545, Russian Federation;AG Phytochemistry, University Witten/Herdecke, Berliner Allee 317/321, Berlin 0-1120, Germany;Institute of Immunology of Russian Federation, Kashirskoye Shosse 24/2, Moscow 115478, Russian Federation

关键词: Ricin;    Mistletoe lectin I;    Chimeric toxin;    Mechanism of action;    MLI;    mistletoe lectin I;    MLA;    mistletoe lectin I A-chain;    RTA;    ricin A-chain;    RTB;    ricin B-chain;    IT;    immunotoxin;    DTT;    dithiotreitol;    PBS;    phosphate-buffered saline;    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(93)81618-A

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Chimeric toxic protein was prepared from the mistletoe lectin I A-chain and ricin B-chain by using the disulfide exchange reaction. Ricin and chimeric protein were indistinguishable in binding to immobilized asialofetuin in ELISA. Chimeric protein was more toxic to Jurkat cells than native mistletoe lectin I, but not so effective as native ricin. In the presence of NH₄Cl, which enhances the toxicity of some toxins and immunotoxins, but does not influence ricin toxicity, both ricin and chimeric toxin had equal cytotoxic activity. The possibility is discussed that the ricin B-chain protects the ricin A-chain (RTA) from degradation during delivering RTA from the cell surface to the place where RTA is translocated into the cytosol.

【 授权许可】

Unknown