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Structure–Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes
Open AccessEditor’s ChoiceArticle

Characterization of Post-Translational Modifications and Cytotoxic Properties of the Adenylate-Cyclase Hemolysin Produced by Various Bordetella pertussis and Bordetella parapertussis Isolates

1
Institut Pasteur, Unité Prévention et Thérapie Moléculaires des Maladies Humaines, 25 rue du Dr Roux, 75724 Paris, CEDEX 15, France
2
Institut Pasteur, Unité de Spectrométrie de Masse pour la Biologie, CNRS/Institut Pasteur USR2000, CITECH, 28 rue du Dr Roux, 75724 Paris, CEDEX 15, France, [email protected] (T.D.)
*
Author to whom correspondence should be addressed.
Current address: Institut Pasteur, Unité Biodiversité et Epidémiologie des Bactéries Pathogènes, 25 rue du Dr Roux, 75724 Paris, CEDEX 15, France.
Academic Editor: Holger Barth
Toxins 2017, 9(10), 304; https://doi.org/10.3390/toxins9100304
Received: 29 August 2017 / Revised: 19 September 2017 / Accepted: 20 September 2017 / Published: 26 September 2017
(This article belongs to the Special Issue Adenylate Cyclase (CyaA) Toxin)
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. View Full-Text
Keywords: adenylate cyclase hemolysin; Bordetella pertussis; Bordetella parapertussis; PTMs adenylate cyclase hemolysin; Bordetella pertussis; Bordetella parapertussis; PTMs
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Bouchez, V.; Douché, T.; Dazas, M.; Delaplane, S.; Matondo, M.; Chamot-Rooke, J.; Guiso, N. Characterization of Post-Translational Modifications and Cytotoxic Properties of the Adenylate-Cyclase Hemolysin Produced by Various Bordetella pertussis and Bordetella parapertussis Isolates. Toxins 2017, 9, 304.

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