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Membrane Activity and Channel Formation of the Adenylate Cyclase Toxin (CyaA) of Bordetella pertussis in Lipid Bilayer Membranes

by Oliver Knapp 1,* and Roland Benz 2,*
1
Department of Life Sciences and Chemistry, Jacobs University, Campus Ring 1, 28759 Bremen, Germany
2
Rudolf-Virchow-Center, University of Würzburg, Versbacher Str. 9, 97078 Würzburg, Germany
*
Authors to whom correspondence should be addressed.
Toxins 2020, 12(3), 169; https://doi.org/10.3390/toxins12030169
Received: 27 January 2020 / Revised: 20 February 2020 / Accepted: 22 February 2020 / Published: 10 March 2020
(This article belongs to the Special Issue RTX Toxins)
The Gram-negative bacterium Bordetella pertussis is the cause of whooping cough. One of its pathogenicity factors is the adenylate cyclase toxin (CyaA) secreted by a Type I export system. The 1706 amino acid long CyaA (177 kDa) belongs to the continuously increasing family of repeat in toxin (RTX) toxins because it contains in its C-terminal half a high number of nine-residue tandem repeats. The protein exhibits cytotoxic and hemolytic activities that target primarily myeloid phagocytic cells expressing the αMβ2 integrin receptor (CD11b/CD18). CyaA represents an exception among RTX cytolysins because the first 400 amino acids from its N-terminal end possess a calmodulin-activated adenylate cyclase (AC) activity. The entry of the AC into target cells is not dependent on the receptor-mediated endocytosis pathway and penetrates directly across the cytoplasmic membrane of a variety of epithelial and immune effector cells. The hemolytic activity of CyaA is rather low, which may have to do with its rather low induced permeability change of target cells and its low conductance in lipid bilayer membranes. CyaA forms highly cation-selective channels in lipid bilayers that show a strong dependence on aqueous pH. The pore-forming activity of CyaA but not its single channel conductance is highly dependent on Ca2+ concentration with a half saturation constant of about 2 to 4 mM. View Full-Text
Keywords: pore formation; adenylate cyclase toxin; CyaA; Bordetella pertussis; membrane interaction; lipid bilayer pore formation; adenylate cyclase toxin; CyaA; Bordetella pertussis; membrane interaction; lipid bilayer
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Knapp, O.; Benz, R. Membrane Activity and Channel Formation of the Adenylate Cyclase Toxin (CyaA) of Bordetella pertussis in Lipid Bilayer Membranes. Toxins 2020, 12, 169.

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