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. 2016 Nov 24;6:37708. doi: 10.1038/srep37708

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Copyright © 2016, The Author(s)

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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Whole cells (WC) of wild-type (W83; left panel) and ΔPorZ (right panel) P. gingivalis strains were proportionately fractionated into periplasm (PP), cytoplasm (CP), cell envelope (CE), outer membrane (OM), inner membrane (IM) and culture medium fractions (Med; 10-fold concentrated); and probed for (a) Rgps, (b) Kgp, (c) PPAD by Western blotting with specific monoclonal antibodies and (d) biotinylated IM protein (MmdC) through reaction with streptavidin conjugated to horseradish peroxidase. The pinpointed and labeled bands correspond to: (a) catalytic domain of RgpA (RgpA_cat) and membrane-type RgpB (mt-RgpB) in the wild type (left panel) and unprocessed pro-RgpA and pro-RgpB in ΔPorZ (right panel); (b) catalytic domain of Kgp (Kgp_cat) in the wild type (left panel) and unprocessed pro-Kgp in ΔPorZ (right panel); (c) mature PPAD and membrane-type PPAD (mt-PPAD) in the wild type (left panel) and unprocessed pro-PPAD in ΔPorZ (right panel); and (d) MmdC in the wild-type (left panel) and ΔPorZ (right panel) strains.