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. 2019 Sep 17;9:13479. doi: 10.1038/s41598-019-49981-6

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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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Proteolytic activity. (A) Casein gel zymography. SDS-PAGE supplemented with 1% casein as a substrate, where a white band is representative for casein digestion. (B) Representative dual-channel gel images of the secretomes of initial (green channel) and host-adapted (red channel) isolate at different OD readings. Differentially abundant proteins were identified by MALDI-TOF-MS/MS (see Fig. S4) (C) aur expression of strains grown in TSB to an optical density of 2.5 and 5.0. The data shown are the means of three independently grown strains and their technical duplicates. Statistical difference between the expression of the initial and host-adapted isolate was determined with unpaired Students t test. (***P < 0.001) (D) Proteolytic cascade cartoon, including the proteins’ molecular weight (MW) and isoelectric point (pI), adapted from Shaw et al.³³. Original, full length zymogel/ 2D-DIGE gels are shown in the Supplementary Information Fig. S7. IN, initial isolate; HA, host-adapted isolate; SspA, glutamyl endopeptidase; SspB, staphopain B; Aur, zinc metalloprotease aureolysin.