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. 2019 Jun 21;9:9022. doi: 10.1038/s41598-019-45440-4

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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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Expression of unfused rPfMSP2 and chimeric rPfMSP2/8. (A) Cartoon of expression constructs for rPfMSP2 and rPfMSP2/8 production. Cysteine residues are indicated by red bars, yellow region indicates Gly-Ser linker domain. (B,C) E. coli lysate at time of induction (T₀) or 3 hours post-induction (T₃) was separated on 10% polyacrylamide gels and rPfMSP2 expression was analyzed by (B) Coomassie Blue staining and (C) immunoblot using anti-PfMSP2 antibody (1:20,000 dilution). (D,E) rPfMSP2/8 expression was analyzed by (D) Coomassie Blue staining and (E) immunoblot as described for rPfMSP2. Asterisks indicate induced rPfMSP2 and rPfMSP2/8 protein products. The T₀ samples served as negative controls for the immunoblot analysis of protein expression.