Rho ADP核糖基化二元C2/C3毒素的纯化及活性

Purification and activity of the Rho ADP-ribosylating binary C2/C3 toxin.

作者信息

Haug Gerd, Barth Holger, Aktories Klaus

机构信息

Albert Ludwigs Universitat Freiburg, Institut fur Experimentelle & Klinische Pharmakologie & Toxikologie, Germany.

出版信息

Methods Enzymol. 2006;406:117-27. doi: 10.1016/S0076-6879(06)06010-1.

DOI:10.1016/S0076-6879(06)06010-1

PMID:16472654

Abstract

C3 exoenzyme from Clostridium limosum, specifically ADP-ribosylates and inactivates Rho GTPases, but not or much less than Rac and Cdc42. To bypass the poor cell accessibility of the exoenzyme, a chimeric fusion toxin was constructed consisting of C3 exoenzyme and the N-terminal adaptor domain of the enzyme component C2I of the actin-ADP-ribosylating Clostridium botulinum C2 toxin. This fusion toxin C2IN-C3 is transported into cells by interaction with the binding and translocation component (C2II) of C2 toxin. Purification and activity of the chimeric toxin is reported.

摘要

来自黏液梭菌的C3外切酶能特异性地对Rho GTP酶进行ADP核糖基化修饰并使其失活，但对Rac和Cdc42的作用很小或几乎没有作用。为了克服外切酶在细胞中难以到达的问题，构建了一种嵌合融合毒素，它由C3外切酶和肌动蛋白ADP核糖基化肉毒梭菌C2毒素的酶组分C2I的N端衔接结构域组成。这种融合毒素C2IN-C3通过与C2毒素的结合和转运组分（C2II）相互作用而被转运到细胞中。本文报道了该嵌合毒素的纯化及活性。