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. 2019 Jul 1;10:2900. doi: 10.1038/s41467-019-10777-x

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© Crown 2019

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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Fig. 1 — Lytic activity of the AHL toxin against horse erythrocytes. a Percentage lysis when each protein was incubated with horse erythrocytes alone and in combination at 1:1 ratios for 1 h. b % Lysis against varying AhlA, AhlB or AhlC concentration, when all three proteins were incubated together for 1 h. The other two proteins were at a fixed concentration of 1 µM. c % lysis against time when erythrocytes were incubated with 500 nM AhlA, AhlB and AhlC (green), or pre-incubated with 500 nM AhlA (black), AhlC (blue), AhlB and AhlC (purple), or AhlA and AhlC (orange), for 1 h before addition of the remaining proteins at time 0. d % lysis against time when erythrocytes were incubated with 500 nM AhlB and AhlC (green), or pre-incubated with 500 nM AhlC (blue) or AhlB (purple) for 1 hour before addition of the second protein at time 0. e TEM negative stain images of AhlB, AhlBC and AhlABC pores in both erythrocytes and liposomes. Scale bars on magnified images represent 10 nm, and pores are highlighted in red circles. f Liposome floatation assay to determine lipid bilayer binding ability of each Ahl toxin component. Membrane binding ability of each AhlA, AhlB and AhlC alone and AhlB+AhlC, and AhlA+AhlB+AhlC (+) was assessed by SDS-PAGE analysis of the six top and six bottom fractions (left to right gel lanes with molecular weight indicated, kDa), together with a control without liposomes (−). A schematic of the ultracentrifuge tube shows the location of the top and bottom fractions and in which fractions liposomes and protein are expected. TEM negative stain EM images are shown of top fractions of AhlB (top), AhlBC (centre) and AhlABC (bottom), with pores circled in red. g SDS-PAGE of soluble (sol) and pelleted (pel) fractions from ultracentrifugation of AhlA, AhlB and AhlC with detergent, alone and in combination. Invitrogen Mark12 ladder (L) is labelled in the first lane. All assays were carried out in triplicate (n = 3) with error bars corresponding to the mean ± standard deviation. Source data are provided as a Source Data file