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Dissecting how bacterial pathogens escape immune destruction and cause respiratory infections in humans is a work in progress. One tactic employed by microbes is to use bacterial adenylate cyclase toxins (ACTs) to disarm immune cells and disrupt cellular signaling in host cells, which facilitates the infection process. Several clinically significant pathogens, such as  Bacillus anthracis  and  Bordetella pertussis , have ACTs that are stimulated by an activator protein in human cells. Research has shown that these bacterial ACTs have evolved distinct ways of controlling their activities, but our understanding of how the  B .  pertussis  ACT does this is limited. In a recent study, O’Brien and colleagues provide new and exciting evidence demonstrating that the regulation of  B .  pertussis  ACT involves conformational switching between flexible and rigid states, which is triggered upon binding the host activator protein. This study increases our knowledge of how bacterial ACTs are unique enzymes, representing a potentially novel class of drug targets that may open new pathways to combat reemerging infectious diseases.

Revealing how an adenylate cyclase toxin uses bait and switch tactics in its activation