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. 2019 Jun 3;4:26. doi: 10.1038/s41541-019-0118-4

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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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Fig. 1 — pT181-Qβ conjugation and treatment paradigm. a A 13-mer peptide, including phosphorylated epitope Threonine 181 (pT181), was synthesized with two glycines (G) and a cysteine (C) and conjugated to the surface-exposed lysine (K, in yellow) residues on the coat proteins of self-assembled Qß RNA bacteriophage VLPs (AB dimers in red, and CC dimers in blue), using SMPH. b An upward mobility shift on a 10% SDS gel indicates the number of peptides conjugated, per bound coat protein. c Non-Tg (n = 6) and rTg4510 (n = 17, separated into two different age- and sex-matched cohorts) were aged to 2 months, received three, bi-weekly intramuscular (im) injections of either: for NonTg: Qß (n = 2) or pT181-Qß (n = 6); for rTg4510: Qß (n = 8) or pT181-Qß (n = 9)