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. 2019 Feb 21;10:891. doi: 10.1038/s41467-019-08869-9

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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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Fig. 3 — Western blot analysis of CPS8-ComP and CPS9V-ComP glycoproteins. Escherichia coli SDB1 cells were prepared co-expressing ComP, PglS, and either the pneumococcal CSP8 or CPS9V. Affinity-purified glycosylated ComP from each strain was analyzed for protein glycosylation via western blot analysis. a–c Western blot analysis of CPS8-ComP bioconjugates compared against ComP alone. a Anti-His channel probing for Hexa-histidine-tagged ComP purified from SDB1 expressing CPS8 in the presence or absence of PglS. b Anti-glycan channel probing for CPS8. c Merged images for panels a and b. d–f Western blot analysis of CPS9V-ComP bioconjugates compared against ComP alone. d Anti-His channel probing for Hexa-histidine-tagged ComP purified from SDB1 expressing CPS9V in the presence or absence of PglS. e Anti-glycan channel probing for CPS9V. f Merged images for panels d and e. The red asterisk indicates samples that were proteinase K treated for 1 h at 55 °C. Source data are provided as a Source Data file