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. 2017 Jul 25;7:6428. doi: 10.1038/s41598-017-06940-3

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© The Author(s) 2017

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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Characterization of the 58 kDa P. acnes surface protein. Concentrated proteins (200 μg) were separated by 2D-electrophoresis. (a) Proteins were detected by silver staining. (b) Fibrinogen binding activity was assessed with biotinylated human fibrinogen (0.1 μg/ml). Lane 1: molecular weight standard. Lane 2: sample separated by 10% SDS-PAGE (1DE) only (50 μg of protein). Lane 3: sample after 2DE. The arrow indicates the spot excised for identification by MALDI-ToF. (c) MALDI-ToF spectrum obtained for the spot of interest. (d) Peptide sequence of the 58 kDa protein with 64% coverage (in bold). The sequence signal is highlighted in gray, the repeated PT domain is underlined, and the LPXTG motif is double-underlined. Based on its binding capacities (to hFg, this study; and to dermatan sulfate^{31, 32}), the 58 kDa protein was abbreviated DsA1.