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Toxins 2017, 9(10), 304; https://doi.org/10.3390/toxins9100304

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, thibaut.douche@pasteur.fr (T.D.)
Current address: Institut Pasteur, Unité Biodiversité et Epidémiologie des Bactéries Pathogènes, 25 rue du Dr Roux, 75724 Paris, CEDEX 15, France.
*
Author to whom correspondence should be addressed.
Academic Editor: Holger Barth
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)
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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. 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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