1. Characterization of Post-Translational Modifications and Cytotoxic Properties of the Adenylate-Cyclase Hemolysin Produced by Various Bordetella pertussis and Bordetella parapertussis Isolates.
- Author
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Bouchez V, Douché T, Dazas M, Delaplane S, Matondo M, Chamot-Rooke J, and Guiso N
- Subjects
- Cell Line, Macrophages drug effects, Protein Processing, Post-Translational, Adenylate Cyclase Toxin genetics, Adenylate Cyclase Toxin metabolism, Adenylate Cyclase Toxin toxicity, Bordetella parapertussis genetics, Bordetella parapertussis metabolism, Bordetella pertussis genetics, Bordetella pertussis metabolism
- Abstract
Bordetella pertussis and Bordetella parapertussis are the causal agents of whooping cough in humans. They produce diverse virulence factors, including adenylate cyclase-hemolysin (AC-Hly), a secreted toxin of the repeat in toxins (RTX) family with cyclase, pore-forming, and hemolytic activities. Post-translational modifications (PTMs) are essential for the biological activities of the toxin produced by B. pertussis . In this study, we compared AC-Hly toxins from various clinical isolates of B. pertussis and B. parapertussis , focusing on (i) the genomic sequences of cyaA genes, (ii) the PTMs of partially purified AC-Hly, and (iii) the cytotoxic activity of the various AC-Hly toxins. The genes encoding the AC-Hly toxins of B. pertussis and B. parapertussis displayed very limited polymorphism in each species. Most of the sequence differences between the two species were found in the C-terminal part of the protein. Both toxins harbored PTMs, mostly corresponding to palmitoylations of the lysine 860 residue and palmoylations and myristoylations of lysine 983 for B. pertussis and AC-Hly and palmitoylations of lysine 894 and myristoylations of lysine 1017 for B. parapertussis AC-Hly. Purified AC-Hly from B. pertussis was cytotoxic to macrophages, whereas that from B. parapertussis was not.
- Published
- 2017
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