槲寄生凝集素I A链与蓖麻毒素B链缀合物和天然毒素的特性比较。

Comparison of properties of mistletoe lectin I A-chain and ricin B-chain conjugate with native toxins.

作者信息

Tonevitsky A G, Shamshiev A T, Agapov I I, Ershova E V, Pfuller U, Pfuller K

机构信息

Institute for Genetics of Microorganisms, Moscow, Russian Federation.

出版信息

FEBS Lett. 1993 Dec 20;336(1):100-2. doi: 10.1016/0014-5793(93)81618-a.

DOI:10.1016/0014-5793(93)81618-a

PMID:8262189

Abstract

Chimeric toxin 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.

摘要

通过二硫键交换反应，由槲寄生凝集素I A链和蓖麻毒素B链制备嵌合毒素蛋白。在酶联免疫吸附测定（ELISA）中，蓖麻毒素和嵌合蛋白与固定化去唾液酸胎球蛋白的结合无法区分。嵌合蛋白对Jurkat细胞的毒性比天然槲寄生凝集素I更强，但不如天然蓖麻毒素有效。在氯化铵存在的情况下，氯化铵可增强某些毒素和免疫毒素的毒性，但不影响蓖麻毒素的毒性，蓖麻毒素和嵌合毒素具有相同的细胞毒活性。文中讨论了一种可能性，即在将蓖麻毒素A链（RTA）从细胞表面递送至RTA转运至胞质溶胶的位置的过程中，蓖麻毒素B链可保护RTA不被降解。