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. 2017 Aug 24;7:9330. doi: 10.1038/s41598-017-09575-6

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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α-helical structures located between residues 600 to 750 of CyaA participate in AC domain translocation and pore formation. (A) Schematic secondary structure of the segment 600 to 750 of CyaA with two putative transmembrane (TM) α-helices predicted by Eisenberg method⁶⁴ and located between residues 607 to 627 and 678 to 698. The amino acid residues selected for substitution are enlarged and colored. (B to E) Biological activities of intact CyaA or its mutant variants were analyzed using CD11b⁻ sheep erythrocytes (B,D) and CD11b⁺ J774A.1 mouse macrophages (C,E). Preparations and analyses of samples were performed as in the legend to Fig. 1. All activities are expressed as percentages of intact CyaA activity and represent average values ± standard deviations from at least three independent determinations performed in duplicate with two different toxin preparations. Significant differences are indicated by asterisks (*p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001).