ArticleScientific reports2017
Stability, structural and functional properties of a monomeric, calcium-loaded adenylate cyclase toxin, CyaA, from Bordetella pertussis.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 44 citations in OpenAlex.
- Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Combinations of colistin and bacteriocins prevent the selection of colistin resistance in Acinetobacter baumannii.Communications biology · 2026Article
- Rare Earth Element-Induced Condensation of the Block V of the Repeats-in-Toxin Domain from CyaA fromLangmuir : the ACS journal of surfaces and colloids · 2025Article
- Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane.The Journal of biological chemistry · 2025Article
- CyaA translocation across eukaryotic cell membranes.Frontiers in molecular biosciences · 2024Article
- B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles.Cell reports methods · 2023Article
- Dynamics and structural changes of calmodulin upon interaction with the antagonist calmidazolium.BMC biology · 2022Article
- Four Cholesterol-Recognition Motifs in the Pore-Forming and Translocation Domains of Adenylate Cyclase Toxin Are Essential for Invasion of Eukaryotic Cells and Lysis of Erythrocytes.International journal of molecular sciences · 2022Article
- Review
- Cholesterol stimulates the lytic activity of Adenylate Cyclase Toxin on lipid membranes by promoting toxin oligomerization and formation of pores with a greater effective size.The FEBS journal · 2021Article
- A High-Affinity Calmodulin-Binding Site in the CyaA Toxin Translocation Domain is Essential for Invasion of Eukaryotic Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Review
- Functional and structural consequences of epithelial cell invasion by Bordetella pertussis adenylate cyclase toxin.PloS one · 2020Article
- Genome Insights of the Plant-Growth Promoting BacteriumFrontiers in microbiology · 2020Article
- Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?Toxins · 2019Review
- Membrane Permeabilization byBiomolecules · 2019Article
- Residues 529 to 549 participate in membrane penetration and pore-forming activity of the Bordetella adenylate cyclase toxin.Scientific reports · 2019Article
- The Adenylate Cyclase (CyaA) Toxin fromToxins · 2019Article
- Bioengineering ofToxins · 2018Review
- Article
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bordetella pertussis, the causative agent of whooping cough, secretes an adenylate cyclase toxin, CyaA, which invades eukaryotic cells and alters their physiology by cAMP overproduction. Calcium is an essential cofactor of CyaA, as it is the case for most members of the Repeat-in-ToXins (RTX) family. We show that the calcium-bound, monomeric form of CyaA, hCyaAm, conserves its permeabilization and haemolytic activities, even in a fully calcium-free environment. In contrast, hCyaAm requires sub-millimolar calcium in solution for cell invasion, indicating that free calcium in solution is involved in the CyaA toxin translocation process. We further report the first in solution structural characterization of hCyaAm, as deduced from SAXS, mass spectrometry and hydrodynamic studies. We show that hCyaAm adopts a compact and stable state that can transiently conserve its conformation even in a fully calcium-free environment. Our results therefore suggest that in hCyaAm, the C-terminal RTX-domain is stabilized in a high-affinity calcium-binding state by the N-terminal domains while, conversely, calcium binding to the C-terminal RTX-domain strongly stabilizes the N-terminal regions. Hence, the different regions of hCyaAm appear tightly connected, leading to stabilization effects between domains. The hysteretic behaviour of CyaA in response to calcium is likely shared by other RTX cytolysins.
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