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. 2020 May 1;5:33. doi: 10.1038/s41541-020-0183-8

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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 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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Fig. 1 — Schematic diagram of OspA fused to a modified H. pylori ferritin through a glycine–serine (GS) linker (A,top). Secondary structure of the transmembrane domain deletion of OspA, in which the carboxy-terminus of OspA where it is attached to ferritin is indicated (purple) (a, bottom left). The ferritin nanoparticle is composed of 24 monomers of H. pylori ferritin (a, bottom middle). The amino-terminal attachment site for OspA on ferritin is highlighted (purple). Structural model of the OspA-ferritin nanoparticle (a, bottom right). Ferritin (green), the GS linker (purple), and OspA (blue) is shown. A SEC profile of OspA-ferritin nanoparticle purification on a Superose 6 column (b). A SDS-PAGE gel of purified OspA-ferritin from E.coli (c). Annotated class averages of OspA-ferritin (318 particles) at 67,000x magnification (d). The ferritin cage appears as a strong circular density with a hollow center in the middle of the averages (green arrow). Each cage is surrounded by numerous, short, uniform spikes of OspA that appear circular or slightly oblong in shape (yellow).