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. 2022 Jan 5;21:6. doi: 10.1186/s12934-021-01728-7

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© The Author(s) 2021

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 1 — Generation of functional SDB1pgl integrants. A Schematic diagram depicting the pSECpgl suicide plasmid. B Strategy for integration of the C. jejuni pgl locus in the SDB1 genome via allelic exchange. C Confirmation of correct integration of the pgl locus via PCR in five SDB1pgl clones. Oligos 1 and 6 align outside of the chosen homology arms, while oligos 2 and 5 align to the pgl locus and the KanR tag, respectively. Formation of amplicons 1&2 and 5&6 is possible only in case of successful integration in the correct location. D SDB1pgl integrants can glycosylate a model carrier protein (G-NetB). SDB1 transformed with a plasmid encoding pgl locus (pACYCpgl) as well as a plasmid encoding pgl locus with a non-functional PglB (pACYCpgl::pglB) were used as positive and negative controls, respectively. His-pulldown followed by western blotting confirms glycoprotein production