Novel bacterial ADP-ribosylating toxins: structure and function

被引：163

作者：

Simon, Nathan C. ^{[1
]}

Aktories, Klaus ^{[2
]}

Barbieri, Joseph T. ^{[1
]}

机构：

[1] Med Coll Wisconsin, Milwaukee, WI 53226 USA

[2] Univ Freiburg, Inst Expt & Clin Pharmacol & Toxicol, D-79104 Freiburg, Germany

来源：

NATURE REVIEWS MICROBIOLOGY | 2014年 / 12卷 / 09期

基金：

美国国家卫生研究院;

关键词：

ISLET-ACTIVATING PROTEIN; COMPLETE GENOME SEQUENCE; ADENOSINE-DIPHOSPHATE-RIBOSYLATION; SMALL NUCLEAR RIBONUCLEOPROTEIN; ESCHERICHIA-COLI ENTEROTOXIN; SALMONELLA-ENTERICA SPVB; HEAT-LABILE ENTEROTOXIN; CELL LINEAGE ABLATION; BOTULINUM C2 TOXIN; RHO GENE-PRODUCT;

D O I：

10.1038/nrmicro3310

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Bacterial ADP-ribosyttransferase toxins (bARTTs) transfer ADP-ribose to eukaryotic proteins to promote bacterial pathogenesis. In this Review, we use prototype bARTTs, such as diphtheria toxin and pertussis toxin, as references for the characterization of several new bARTTs from human, insect and plant pathogens, which were recently identified by bioinformatic analyses. Several of these toxins, including cholix toxin (ChxA) from Vibrio cholerae, SpyA from Streptococcus pyogenes, HopU1 from Pseudomonas syringoe and the Tcc toxins from Photorhabdus luminescens, ADP-ribosylate novel substrates and have unique organizations, which distinguish them from the reference toxins. The characterization of these toxins increases our appreciation of the range of structural and functional properties that are possessed by bARTTs and their roles in bacterial pathogenesis.

引用

页码：599 / 611

页数：13

共 203 条

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