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. 2020 Oct 13;10:17095. doi: 10.1038/s41598-020-74105-w

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© The Author(s) 2020

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 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/.

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Covalent binding is caused by interaction of SpyCatcher with SpyTag. The table at the top indicates the approximate expected sizes of conjugated and unconjugated proteins. Bottom: duplicate anti-HBcAg (left) and anti-GFP (right) western blots of total soluble protein obtained from leaves co-expressing the proteins indicated. Higher molecular weight multimers of tandem core proteins are visible in the anti-HBcAg blot for all constructs, but these are only visible in the anti-GFP blot when the SpyCatcher/SpyTag interaction can take place (first lane), indicating covalent binding of GFP to HBcAg. Monomers of GFP-ST and GFP-SC are visible in the anti-GFP blot (arrows 5 and 6, respectively) along with bands of an unknown nature (marked “?”) which cannot be GFP bound to tHBcAg since these bands are not present on the anti-HBcAg blot. Blots cropped for clarity, for uncropped blots see Supplementary Fig. S4.