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. 2020 Aug 27;16:313. doi: 10.1186/s12917-020-02527-9

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. 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 in a credit line to the data.

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Fig. 1 — The schematic structure (a) and SDS-PAGE (b) of four recombinant Cap-CRT fusion proteins. a Fragments were used for constructing the recombinant proteins. Blue squares represent completely cap of PCV2 and truncated calreticulin. GGGGS in grey are linkers between cap and calreticulin. Each fragment is encoded by BamHI and XhoI, respectively. b Solubility of rP4C, rC4P, rP5F and rF5P induced by IPTG at 37 °C. M: protein ladder; Lane 1,3,5,7: precipitate of pET-28a-rP4C/rC4P/rV5P/rF5P; Lane 2,4,6,8: supernatant of pET-28a-rP4C/rC4P/rV5P/rF5P