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. 2015 Feb 21;14:88. doi: 10.1186/s12936-015-0553-2

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© Saetear et al.; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Backscattering interferometry detects the PfEBA175-GYPA interaction on intact unmodified erythrocytes. (A) The entire ectodomain of PfEBA175 was expressed and purified as a Cd4-tagged monomer and resolved under reducing conditions by SDS-PAGE. Coomassie staining revealed a single band of the expected size (185 kDa). (B) Quantitation of PfEBA175 binding to intact unmodified erythrocytes at equilibrium using BSI. Erythrocytes that were either neuraminidase-treated (blue squares) or pre-coated with anti-GYPA monoclonal antibody BRIC256 (red circles) were used as control samples. Data points are means ± SD from three independent experiments.