The cytolethal distending toxin B sub-unit of Helicobacter hepaticus is a Ca2+- and Mg2+-dependent neutral nuclease

被引：19

作者：

Dassanayake, RP

Griep, MA

Duhamel, GE

机构：

[1] Univ Nebraska, Dept Vet & Biomed Sci, Lincoln, NE 68583 USA

[2] Univ Nebraska, Dept Chem, Lincoln, NE 68588 USA

[3] Univ Nebraska, Ctr Biotechnol, Lincoln, NE USA

来源：

FEMS MICROBIOLOGY LETTERS | 2005年 / 251卷 / 02期

关键词：

Helicobacter hepaticus; cytolethal distending toxin; cdtB; toxin; nuclease;

D O I：

10.1016/j.femsle.2005.08.005

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The cytolethal distending toxin B (CdtB) of the mouse pathogen Helicobacter hepaticus has cation binding and DNA catalysis residues in common with members of the mammalian deoxyribonuclease I (DNase I) family. The purpose of the present study was to characterize CdtB nuclease. To establish optimal digestion conditions and to evaluate co-factor requirements, a novel and sensitive fluorometric assay that quantitatively determines double stranded DNA digestion was developed. Although the Ca2+- and Mg2+-dependence and neutral properties of CdtB were similar to DNase I, hydrolysis of DNA by CdtB was approximately 100-fold less active than DNase I and was considerably more resistant to inhibition by ZnCl2 and G-actin. (C) 2005 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.

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页码：219 / 225

页数：7

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