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. 2018 Jan 18;8:1118. doi: 10.1038/s41598-017-19063-6

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© The Author(s) 2018

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, purification, and biophysical analyses of recombinant proteins. (a) SDS-PAGE (12%) of yPvCSP-All_FL and yPvCSP-All_CT proteins, stained with Coomassie blue under reducing conditions. (b) Immunoblotting analyses of recombinant yPvCSP-All_FL and yPvCSP-All_CT. (1). Anti-histidine tag mAb (diluted 1:1,000, GE Healthcare); (2). Anti-PvCSP-VK210 mAb (diluted 1:1,000) 3. Anti-PvCSP-VK247 mAb (diluted 1:11,000). NR and R: proteins under non-reducing and reducing conditions (with 2-mercaptoethanol), respectively; (c) The purity of proteins yPvCSP-All_FL and yPvCSP-All_CT, after a combination of chromatographic separations, was analysed by RP-HPLC. The gradient elution was developed with 0.1% TFA in water and 0.1% TFA in 90% acetonitrile at 22 °C, and a rate of 1 mL/min for 30 minutes on a C₁₈ column (Phenomenex). MW: molecular weight. (d) The secondary structure of yPvCSP-All_FL and yPvCSP-All_CT was analysed by a circular dichroism (CD) spectrum. The CD spectrum of the recombinant proteins was recorded from 190 to 260 nm using a JASCO-J815 spectropolarimeter.