Clinical significance ADP-ribosylation

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crystal structure of diphtheria toxin. pdb: 1mdt


upon activation, bares adp-ribosylate number of eukaryotic proteins; such mechanism crucial instigation of diseased states associated adp-ribosylation. gtp-binding proteins, in particular, well-established in bares pathophysiology. examples, cholera , heat-labile enterotoxin target α-subunit of gs of heterotrimeric gtp-binding proteins. α-subunit adp-ribosylated, permanently in active , gtp-bound state; subsequent activation of intracellular cyclic amp stimulates release of fluid , ions intestinal epithelial cells. furthermore, c3 adp-ribosylates gtp-binding proteins rho , ras, , pertussis adp-ribosylates gi, go, , gt. in diphtheria, adp-ribosylates ribosomal elongation factor ef-2, attenuates protein synthesis.


there variety of bacteria employ bares in infection: cholera of vibrio cholera; heat-labile enterotoxin of e.coli; exotoxin of pseudomonas aeruginosa; pertussis toxin of b. pertussis; c3 toxin of c. botulinum; , diphtheria toxin of corynebacterium diphtheriae.








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