ArticleThe Journal of biological chemistry2025
Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane.
Article in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Folding of the nonacylated acylation domain of the adenylate cyclase toxin is templated by its C-terminal RTX domain.The Journal of biological chemistry · 2026Article
- The Minimal Folding Motif of the Repeat-in-Toxin Domain of Adenylate Cyclase Toxin.Langmuir : the ACS journal of surfaces and colloids · 2026Article
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7 authors.
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Abstract
Acylated domains (ADs), like that of the Bordetella pertussis adenylate cyclase toxin (CyaA), are structures found in all pore-forming toxins from the family of Repeat-in-ToXin (RTX) proteins. These AD segments are fatty-acylated on ε-amino groups of conserved lysine residues, such as the K860 and K983 residues of CyaA. The ε-amide-linked acyl chains are essential for toxin activity and promote irreversible membrane insertion of the CyaA molecule, thus enabling the toxin to translocate its N-terminal adenyl cyclase enzyme domain into the host cell cytoplasm. In parallel, the membrane-inserted CyaA molecules can oligomerize into cation-selective pores in the plasma membrane. Here, we show that the attached acyl chains are not only crucial for membrane insertion of the toxin but also play an important role in CyaA folding. We demonstrate that assembly of the noncanonical β-roll structure in the C-terminal segment of the AD of CyaA is cooperatively directed by the Ca
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