Match each bacterial pathogen's primary virulence toxin with its precise molecular mechanism of action.
- Corynebacterium diphtheriae exotoxinInactivates elongation factor 2 (EF-2) to inhibit cellular protein synthesis
- Vibrio cholerae enterotoxinADP-ribosylates Gs protein to increase intracellular cAMP levels
- Clostridium tetani neurotoxinCleaves SNARE proteins, preventing the release of inhibitory neurotransmitters
- Staphylococcus aureus TSST-1Cross-links T-cell receptors to MHC class II molecules, triggering a cytokine storm
Answer
The correct matches align specific bacterial toxins with their cellular targets: Corynebacterium diphtheriae exotoxin inactivates EF-2, Vibrio cholerae enterotoxin ADP-ribosylates Gs protein, Clostridium tetani neurotoxin cleaves SNARE proteins, and Staphylococcus aureus TSST-1 cross-links TCR to MHC class II.
Each exotoxin has a highly specific cellular target that dictates its pathophysiology. Diphtheria toxin halts protein synthesis via EF-2 inactivation, causing pseudomembrane formation. Cholera toxin perpetually activates adenylate cyclase by targeting Gs, leading to secretory diarrhea. Tetanospasmin prevents the release of GABA and glycine by cleaving SNARE proteins, resulting in spastic paralysis. TSST-1 is a superantigen that bridges MHC class II and T-cell receptors without specific antigen processing, leading to toxic shock syndrome.
Step-by-Step Solution
Key Concept
Bacterial Exotoxin Mechanisms