ADP-ribosyl transferase activity?
(A) Pertussis toxin
(B) Diphtheria toxin
(C) Pseudomonas Exotoxin A
(D) S. aureus α-toxin
The correct answer to Q.37 is (D) S. aureus α-toxin, which forms membrane pores rather than transferring ADP-ribose to host proteins.
Correct Answer
Option (D) S. aureus α-toxin lacks ADP-ribosyl transferase activity. This pore-forming β-barrel toxin lyses host cells by creating 1-2 nm transmembrane channels, disrupting membrane potential and causing necrosis, unlike the enzymatic ADP-ribosylation of AB toxins A, B, C.
Option Analysis
(A) Pertussis toxin: Has ADP-Ribosyl Activity
Pertussis toxin (PT) ADP-ribosylates Gαi proteins at Cys351 using NAD+, inhibiting Gi signaling and causing uncontrolled cAMP elevation, leading to whooping cough symptoms.
(B) Diphtheria toxin: Has ADP-Ribosyl Activity
Diphtheria toxin ADP-ribosylates EF-2 at diphthamide residue, halting protein synthesis by blocking translocation; its A subunit catalyzes this in cytosol after receptor-mediated entry.
(C) Pseudomonas Exotoxin A: Has ADP-Ribosyl Activity
ExoA ADP-ribosylates EF-2 like diphtheria toxin, inhibiting elongation factor function and causing cell death; common in Pseudomonas aeruginosa infections.
(D) S. aureus α-toxin: No ADP-Ribosyl Activity
α-Toxin (also α-hemolysin) oligomerizes into heptameric pores on target membranes (erythrocytes, leukocytes), not using ADP-ribosylation; classified as a pore-forming toxin.
| Option | Toxin | Mechanism | ADP-Ribosyl Activity? |
|---|---|---|---|
| (A) | Pertussis toxin | Gαi modification | Yes |
| (B) | Diphtheria toxin | EF-2 inhibition | Yes |
| (C) | Pseudomonas ExoA | EF-2 inhibition | Yes |
| (D) | S. aureus α-toxin | Pore formation | No |


