Pertussis toxin (PT) is a multi-subunit complex toxin that possesses one active subunit(A) and five binding subunits (B5). PT enters the mammalian cells via endocytosis by attaching itself to the glycosylated molecules on the surface of these cells.

Inactive toxin form released from B. pertussis.

Pertussis toxin from Bordetella pertussis has been used: as a blocker of the G_αi subunit of the chemokine (CXCR4) receptor to measure the intracellular Ca²⁺ in breast cancer cell lines, to characterize the Gi signaling involved in ADP-induced tissue factor (TF) and P-selectin exposure, to induce autoimmune vasculitis in a rat model

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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