ArticleThe Journal of biological chemistry2026
Folding of the nonacylated acylation domain of the adenylate cyclase toxin is templated by its C-terminal RTX domain.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Adenylate cyclase toxin (CyaA) is a key virulence factor secreted by the whooping cough-causing bacterium Bordetella pertussis. Its acylation domain (AD) is a conserved functional domain amongst various pore-forming toxins. In CyaA, AD connects the C-terminal repeats-in-toxin (RTX) domain to the N-terminal functional domains, such as the hydrophobic domain and the adenylate cyclase domain, and its proper folding is important for the acquisition of the active conformation and full toxin activity of CyaA. However, the mechanism of AD folding remains elusive. Using single-molecule optical tweezers, here we investigated the folding pathway of nonacylated AD in the context of a truncated RTX scaffold. We showed that a truncated RTX construct, ΔRTX-i/v, in which the N-terminal part of RTX-i was connected to the C-terminal part of RTX-v, is folded upon binding of Ca
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