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. 2017 Jul 3;7:4524. doi: 10.1038/s41598-017-04767-6

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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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DENV2 sRecE dimer assembly on Ni²⁺-coated surfaces. (A) Indicated amounts of DENV2 sRecE were loaded and reloaded on Ni²⁺-coated plates and analyzed for monomeric (4G2) or dimeric protein structures (2D22). Increased dimer formation is displayed as the 2D22/4G2 signal ratio. (B) The same assay was performed with EDE1 (A11, B7), EDE2 (C8, C10) and C) 3F9 and 1M7 mAbs. No antibody signals were detected when no protein was loaded or reloaded and groups 500 + 0 and 500 + 500 were statistically compared by student T-test (p < 0.05).