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Detection of ADP-Ribosylating Bacterial Toxins

  • Chen Chen
  • Joseph T. Barbieri
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 1813)

Abstract

Many bacterial toxins catalyze the transfer of ADP-ribose from nicotinamide adenine dinucleotide (NAD) to a host protein. Greater than 35 bacterial ADP-ribosyltransferase toxins (bARTTs) have been identified. ADP-ribosylation of host proteins may be specific or promiscuous. Despite this diversity, bARTTs share a common reaction mechanism, three-dimensional active site structure, and a conserved active site glutamic acid. Here, we describe how to measure the ADP-ribosylation of host proteins as purified proteins or within a cell lysate.

Key words

Bacterial toxins Toxins ADP-ribosyltransferase NAD-glycohydrolase 32P-NAD Biotin-NAD 

Notes

Acknowledgments

JTB laboratory is supported by grants from the NIH: AI-030162 and AI-118389.

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Microbiology and ImmunologyMedical College of WisconsinMilwaukeeUSA

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