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Nat Rev Microbiol. 2014 Sep;12(9):599-611. doi: 10.1038/nrmicro3310. Epub 2014 Jul 14.

Novel bacterial ADP-ribosylating toxins: structure and function.

Author information

1
Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA.
2
Institute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.

Abstract

Bacterial ADP-ribosyltransferase 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 syringae 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.

PMID:
25023120
PMCID:
PMC5846498
DOI:
10.1038/nrmicro3310
[Indexed for MEDLINE]
Free PMC Article

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