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Toxins 2015, 7(5), 1486-1496;

Membrane-Pore Forming Characteristics of the Bordetella pertussis CyaA-Hemolysin Domain

Bacterial Protein Toxin Research Cluster, Institute of Molecular Biosciences, Mahidol University, Salaya Campus, Nakornpathom 73170, Thailand
Laboratory of Theoretical and Computational Biophysics, Department of Physics, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand
Department of Biopharmacy, Faculty of Pharmacy, Silpakorn University, Nakornpathom 73000, Thailand
Laboratory of Molecular Biophysics and Structural Biochemistry, Biophysics Institute for Research and Development (BIRD), Bangkok 10160, Thailand
Author to whom correspondence should be addressed.
Academic Editor: Shin-ichi Miyoshi
Received: 17 March 2015 / Revised: 13 April 2015 / Accepted: 21 April 2015 / Published: 30 April 2015
(This article belongs to the Section Bacterial Toxins)
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Previously, the 126-kDa Bordetella pertussis CyaA pore-forming/hemolysin (CyaA-Hly) domain was shown to retain its hemolytic activity causing lysis of susceptible erythrocytes. Here, we have succeeded in producing, at large quantity and high purity, the His-tagged CyaA-Hly domain over-expressed in Escherichia coli as a soluble hemolytically-active form. Quantitative assays of hemolysis against sheep erythrocytes revealed that the purified CyaA-Hly domain could function cooperatively by forming an oligomeric pore in the target cell membrane with a Hill coefficient of ~3. When the CyaA-Hly toxin was incorporated into planar lipid bilayers (PLBs) under symmetrical conditions at 1.0 M KCl, 10 mM HEPES buffer (pH 7.4), it produced a clearly resolved single channel with a maximum conductance of ~35 pS. PLB results also revealed that the CyaA-Hly induced channel was unidirectional and opened more frequently at higher negative membrane potentials. Altogether, our results first provide more insights into pore-forming characteristics of the CyaA-Hly domain as being the major pore-forming determinant of which the ability to induce such ion channels in receptor-free membranes could account for its cooperative hemolytic action on the target erythrocytes. View Full-Text
Keywords: CyaA-Hly; Bordetella pertussis; cooperative action; hemolytic activity; oligomeric pores; single channels CyaA-Hly; Bordetella pertussis; cooperative action; hemolytic activity; oligomeric pores; single channels

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Kurehong, C.; Kanchanawarin, C.; Powthongchin, B.; Katzenmeier, G.; Angsuthanasombat, C. Membrane-Pore Forming Characteristics of the Bordetella pertussis CyaA-Hemolysin Domain. Toxins 2015, 7, 1486-1496.

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