Pertussis toxin

Pertussis (Pertussis) toxin (PTX) is a protein isolated from the bacterium Bordatella (Bordatella) coccobaccillus. The toxin is excreted in a non-active state. When the B oligomer of the bacterium, Bordatella coccobacillus, comes in contact with the cell membrane, an S1 subunit of its A protomer is activated. This activation may be mediated by glutathione and/or ATP.

Inactive toxin form released from B. pertussis.

Pertussis toxin from Bordetella pertussis has been used: to enhance cardiac myosin immunization of rats to induce myocarditis; to break down the blood–brain barrier in the Cuprizone and cuprizone/MOG-EAE model; as an inhibitor of Gαi signaling

The toxin is released from B. pertussis in an inactive form. When the pertussis toxin B oligomer binds to the cell membrane, the S1 subunit of its A protomer becomes activated, perhaps through the action of glutathione and ATP. A protocol for activating pertussis toxin in vitro is given by Kaslow, et al.

Pertussis toxin catalyzes the ADP-ribosylation of the α subunits of the heterotrimeric guanine nucleotide regulatory proteins G_i, G_o, and G_t.

Pertussis toxin catalyzes the ADP-ribosylation of the α subunits of the heterotrimeric guanine nucleotide regulatory proteins G_i, G_o, and G_t. This prevents the G protein heterotrimers from interacting with receptors, thus blocking their coupling and activation. Since the G_α subunits remain in their GDP-bound, inactive state, they are unable to inactivate adenylyl cyclase or open K⁺ channels.

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Aseptically filled solution in 50% glycerol, containing 50 mM TRIS, 10 mM glycine, 0.5 M NaCl, pH 7.5