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. 2019 Aug 12;9:11619. doi: 10.1038/s41598-019-48031-5

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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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(a) Schematic representation of fibronectin binding protein A (FnBPA) from S. aureus 8325-4 (not to scale). The N-terminus contains a signal sequence (S) followed by the A domain, which contains the N2N3 binding site for fibrinogen (Fg). Adjacent to the A domain are eleven repeats that bind to fibronectin (Fn). The C-terminus contains a proline-rich repeat (PRR), wall (W) and membrane (M) spanning domains. Numbers across the bottom correspond to amino acid residues. The asterisks above the boxes indicate the repeat regions with reported amino acid substitutions (at positions 652, 782 and 786). Optical microscopy images of Lactococcus lactis expressing (L. lactis A, FnBPA⁺) or not expressing (L. lactis 0, FnBPA⁻) cell wall associated FnBPA following incubation on (b) Fn-coated glass slides and (c) Fg-coated glass slides. Slides were coated with 100 µg/mL of Fn or Fg.