Chemical reporters for exploring ADP-ribosylation and AMPylation at the host-pathogen interface

被引:10
|
作者
Westcott, Nathan P. [1 ]
Hang, Howard C. [1 ]
机构
[1] Rockefeller Univ, Lab Chem Biol & Microbial Pathogenesis, New York, NY 10065 USA
关键词
ADENOSINE-DIPHOSPHATE RIBOSYLATION; PROTEOME-WIDE IDENTIFICATION; ESCHERICHIA-COLI; BINDING-PROTEINS; RAT-LIVER; POLY(ADP-RIBOSE); SUBSTRATE; POLYMERASE; NAD; RIBOSYLTRANSFERASES;
D O I
10.1016/j.cbpa.2014.10.002
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Bacterial pathogens secrete protein toxins and effectors that hijack metabolites to covalently modify host proteins and interfere with their function during infection. Adenosine metabolites, such as nicotinamide adenine dinucleotide (NAD) and adenosine triphosphate (ATP), have in particular been co-opted by these secreted virulence factors to reprogram host pathways. While some host targets for secreted virulence factors have been identified, other toxin and effector substrates have been elusive, which require new methods for their characterization. In this review, we focus on chemical reporters based on NAD and ATP that should facilitate the discovery and characterization of adenosine diphosphate (ADP)-ribosylation and adenylylation/AMPylation in bacterial pathogenesis and cell biology.
引用
收藏
页码:56 / 62
页数:7
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