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. 2018 Feb 7;8:2555. doi: 10.1038/s41598-018-20863-7

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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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Peptides can be inserted into loop regions from structurally related backbone pilus proteins. (A) The structures of the backbone pilus proteins found in serotype M18/T18 and serotype M28/T28 were modelled onto the Spy0128 (serotype M1/T1) crystal structure (3B2M) using the Swiss PDB modeling server⁵³. Despite low amino acid sequence identities, the models predicted conserved structures, which allowed the identification of loop regions equivalent to those analysed in Spy0128 (M1/T1). The model peptide Ova_324–339 was inserted into the βE-βF loop region of M18_Spy0128 using the same cloning strategy as for M1_Spy0128. (B) Western blot analysis of L. lactis cell wall extracts (CWE) with antiserum specific for M18_Spy0128. (C) Flow cytometry analysis with anti-M18_Spy0128 antiserum shows expression of M18_Spy0128 on the surface of L. lactis, but with notably reduced expression after insertion of peptides into the βE-βF loop region. Error bars show the standard deviation from 3 independent experiments. ***p<0.0005; one-way ANOVA followed by a Holm-Sidak test.