Detection of ADP-Ribosylating Bacterial Toxins

Chen Chen; Joseph T Barbieri

doi:10.1007/978-1-4939-8588-3_20

Detection of ADP-Ribosylating Bacterial Toxins

Methods Mol Biol. 2018:1813:287-295. doi: 10.1007/978-1-4939-8588-3_20.

Authors

Chen Chen¹, Joseph T Barbieri²

Affiliations

¹ Microbiology and Immunology, Medical College of Wisconsin, Milwaukee, WI, USA.
² Microbiology and Immunology, Medical College of Wisconsin, Milwaukee, WI, USA. Jtb01@mcw.edu.

PMID: 30097876
DOI: 10.1007/978-1-4939-8588-3_20

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.

Keywords: 32P-NAD; ADP-ribosyltransferase; Bacterial toxins; Biotin-NAD; NAD-glycohydrolase; Toxins.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

ADP Ribose Transferases / chemistry
ADP-Ribosylation*
Bacterial Toxins / chemistry
Bacterial Toxins / isolation & purification*
Catalysis
Models, Molecular
Molecular Biology / methods*
NAD / chemistry*

Substances

Bacterial Toxins
NAD
ADP Ribose Transferases