Free immunotoxin mechanism Image
Denise C.
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Image Generated: 30th October 2024
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**Nemesis and DTx Mechanism:** Nemesis is a recombinant immunotoxin that replaces the cell-binding domain of diphtheria toxin (DTx) with an anti-CD9 antibody fragment. Upon binding to target cells, Nemesis is internalized through clathrin-coated endocytosis. The acidic environment of early endosomes induces a conformational change in the toxin, allowing the B chain to insert into the membrane and form a translocation pore. This pore facilitates the entry of the catalytic A chain (DTxA) into the cytosol, where it unfolds due to the narrow pore size. The disulfide bond linking the A and B chains is cleaved, enabling the active DTxA to refold in the cytosol. Once in the cytosol, DTxA transfers an ADP-ribose group from NAD+ to a diphthamide residue in eukaryotic elongation factor-2 (eEF2), effectively inactivating it. This inactivation halts protein synthesis, leading to cellular apoptosis. In the context of proteasomal activity, DTxA is normally targeted for degradation, but the presence of proteasome inhibitors can enhance the cytotoxic effect of Nemesis by preventing DTxA degradation and increasing its activity within the target cells.Tags
immunotoxin mechanismprotein synthesiscellular apoptosis
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