An ELISA method to estimate the mono ADP-ribosyltransferase activities: e.g in pertussis toxin and vaccines

被引:8
作者
Asokanathan, Catpagavalli [1 ]
Tierney, Sharon [1 ]
Ball, Christina R. [2 ]
Buckle, George [1 ]
Day, Ami [1 ]
Tanley, Simon [1 ]
Bristow, Adrian [2 ]
Markey, Kevin [1 ]
Xing, Dorothy [1 ]
Yuen, Chun-Ting [2 ]
机构
[1] Blanche Lane, Div Bacteriol, Potters Bar EN6 3QG, Herts, England
[2] Natl Inst Biol Stand & Controls, Blanche Lane, TDI, Potters Bar EN6 3QG, Herts, England
关键词
Mono ADP-Ribosyltransferase; Macro domain; Pertussis toxin; Pertussis vaccines; HISTAMINE SENSITIZATION TEST; VITRO ASSAY SYSTEM; RIBOSYLATION; PROTEINS; SUBSTRATE; DOMAIN;
D O I
10.1016/j.ab.2017.10.025
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
ADP-ribosyltransferase activities have been observed in many prokaryotic and eukaryotic species and viruses and are involved in many cellular processes, including cell signalling, DNA repair, gene regulation and apoptosis. In a number of bacterial toxins, mono ADP-ribosyltransferase is the main cause of host cell cytotoxicity. Several approaches have been used to analyse this biological system from measuring its enzyme products to its functions. By using a mono ADP-ribose binding protein we have now developed an ELISA method to estimate native pertussis toxin mono ADP-ribosyltransferase activity and its residual activities in pertussis vaccines as an example. This new approach is easy to perform and adaptable in most laboratories. In theory, this assay system is also very versatile and could measure the enzyme activity in other bacteria such as Cholera, Clostridium, E. coli, Diphtheria, Pertussis, Pseudomonas, Salmonella and Staphylococcus by just switching to their respective peptide substrates. Furthermore, this mono ADP-ribose binding protein could also be used for staining mono ADP-ribosyl products resolved on gels or membranes.
引用
收藏
页码:15 / 19
页数:5
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