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. 2018 Jun 12;8:8949. doi: 10.1038/s41598-018-27223-5

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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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A-LPS modification of PPAD in sorting type I and II isolates of P. gingivalis. Cells of P. gingivalis sorting type I and II isolates were cultured in BHI and, subsequently, extracted with Triton X-114. Upon phase separation at 37 °C, proteins in the detergent-rich (T) and aqueous (A) phases were analyzed by LDS-PAGE and Western blotting. In panel A immunodetection was performed with an A-LPS-specific monoclonal antibody. Panel B shows a dual-labeling image upon immunodetection with the A-LPS-specific monoclonal antibody (green signal) and a PPAD-specific rabbit antibody (red signal). Bands representing the A-LPS-modified PPAD species of ~75–85-kDa PPAD are boxed in both panels. Names of sorting type I isolates are underlined. Molecular weights of marker proteins are indicated. The full-length blot is presented in Figure S1. Please note that the order of ‘A’- and ‘T’-labeled lanes is inversed compared to Fig. 2 as samples were loaded in a different order.