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. 2017 Aug 11;7:7913. doi: 10.1038/s41598-017-08489-7

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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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Impact of LprG O-mannosylation on the release of the LprG/LAM complex in M. smegmatis. Similar amounts of LprG-His or LprG-His T231A purified from either culture medium or bacterial cells were separated by SDS-PAGE, transferred onto membranes and revealed using anti-LAM or anti-His antibodies. The genetic backgrounds in which the protein was produced are indicated. The upper band revealed by the anti-His antibody is a non-specific cross-reacting protein. The signal intensity for LAM was quantified and plotted in the graph below the Western blot image. This blot is representative of three independent experiments.