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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 protein O-mannosylation on LAM exposition to the bacterial cell surface and release of the LprG/LAM complex. (A) FACS analyses of LAM staining on the surface of the various M. tuberculosis strains. The bar graph values correspond to the median fluorescence value after normalization to H37Rv. Results are representative of two independent experiments. *P < 0.05. (B) Western-blot analyses of LAM associated with LprG in WT M. tuberculosis or Δpmt mutant. Similar amounts of LprG-His protein purified from the bacteria or culture medium were separated by SDS-PAGE. After transfer, the LAM or LprG-His molecules were revealed using the anti-LAM antibody CS-35 or an anti-His antibody. Blots are representative of at least three independent experiments.