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Cholera toxin consists of a single A subunit surrounded by five B subunits. The B subunits are responsible for the attachment of the native toxin to ganglioside GM1 on mammalian cell surfaces, and facilitate translocation of the A subunit. The A subunit catalyzes the ADP-ribosylation of an arginine residue on the a subunit of G proteins, reducing intrinsic GTPase activity and activating the a subunit. ADP-ribosylation of other proteins such as human red cell Ca-ATPase has also been reported. Cholera toxin must interact with ADP-ribosylation factor (ARF) for maximal activity.
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Regulatory Status |
RUO – Research Use Only |
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