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Toxins 2017, 9(10), 295; https://doi.org/10.3390/toxins9100295

Understanding the Mechanism of Translocation of Adenylate Cyclase Toxin across Biological Membranes

Biofisika Insititute (UPV/EHU, CSIC) and Department of Biochemistry and Molecular Biology, University of Basque Country (UPV/EHU), 48080 Bilbao, Spain
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Academic Editor: Alexandre Chenal
Received: 22 August 2017 / Revised: 13 September 2017 / Accepted: 15 September 2017 / Published: 21 September 2017
(This article belongs to the Special Issue Adenylate Cyclase (CyaA) Toxin)
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Abstract

Adenylate cyclase toxin (ACT) is one of the principal virulence factors secreted by the whooping cough causative bacterium Bordetella pertussis, and it has a critical role in colonization of the respiratory tract and establishment of the disease. ACT targets phagocytes via binding to the CD11b/CD18 integrin and delivers its N-terminal adenylate cyclase (AC) domain directly to the cell cytosol, where it catalyzes unregulated conversion of cytosolic ATP into cAMP upon activation by binding to cellular calmodulin. High cAMP levels disrupt bactericidal functions of the immune cells, ultimately leading to cell death. In spite of its relevance in the ACT biology, the mechanism by which its ≈400 amino acid-long AC domain is transported through the target plasma membrane, and is released into the target cytosol, remains enigmatic. This article is devoted to refresh our knowledge on the mechanism of AC translocation across biological membranes. Two models, the so-called “two-step model” and the recently-proposed “toroidal pore model”, will be considered. View Full-Text
Keywords: Adenylate cyclase; RTX toxin; protein translocation; phospholipase activity; model membranes Adenylate cyclase; RTX toxin; protein translocation; phospholipase activity; model membranes
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Ostolaza, H.; Martín, C.; González-Bullón, D.; Uribe, K.B.; Etxaniz, A. Understanding the Mechanism of Translocation of Adenylate Cyclase Toxin across Biological Membranes. Toxins 2017, 9, 295.

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