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. 2019 Nov 18;9:16978. doi: 10.1038/s41598-019-53334-8

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© The Author(s) 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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Recombinant proteins used in the study. (a) Schematic representation of the VAR2CSA protein organization and sequence boundaries of the multi-domain constructs used in this study. The extracellular part of VAR2CSA from P. reichenowi comprises a truncated gene encoding an NTS, two DBL domains (DBL1x to DBL2x) and a truncated ID2 (tID2). The first and last amino-acids of each construct are depicted as they appear within the exon 1 sequence of VAR2CSA from P. reichenowi. P. falciparum comprises an N-terminal sequence (NTS), six Duffy Binding-Like domains (DBL1x to DBL6ε) interspaced by four inter-domain regions (ID1 to ID4). The ID2 region includes the CIDR_PAM domain. (b) SDS-PAGE under reducing conditions followed by Coomassie blue staining of the VAR2CSA-derived purified proteins. His-tagged recombinant proteins were purified in a 2-phase process comprising metallo-affinity and gel filtration chromatography. MW: molecular weight. Three independent gels were run and are displayed.