Cholera toxin: an intracellular journey into the cytosol by way of the endoplasmic reticulum

Cholera toxin (CT), an AB(5)-subunit toxin, enters host cells by binding the ganglioside GM1 at the plasma membrane (PM) and travels retrograde through the trans-Golgi Network into the endoplasmic reticulum (ER). In the ER, a portion of CT, the enzymatic A1-chain, is unfolded by protein disulfide is...

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Veröffentlicht in:Toxins 2010-03, Vol.2 (3), p.310-325
Hauptverfasser: Wernick, Naomi L B, Chinnapen, Daniel J-F, Cho, Jin Ah, Lencer, Wayne I
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Sprache:eng
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Zusammenfassung:Cholera toxin (CT), an AB(5)-subunit toxin, enters host cells by binding the ganglioside GM1 at the plasma membrane (PM) and travels retrograde through the trans-Golgi Network into the endoplasmic reticulum (ER). In the ER, a portion of CT, the enzymatic A1-chain, is unfolded by protein disulfide isomerase and retro-translocated to the cytosol by hijacking components of the ER associated degradation pathway for misfolded proteins. After crossing the ER membrane, the A1-chain refolds in the cytosol and escapes rapid degradation by the proteasome to induce disease by ADP-ribosylating the large G-protein Gs and activating adenylyl cyclase. Here, we review the mechanisms of toxin trafficking by GM1 and retro-translocation of the A1-chain to the cytosol.
ISSN:2072-6651
2072-6651
DOI:10.3390/toxins2030310