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. 2018 Jan 11;28(4):233–244. doi: 10.1093/glycob/cwx110

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© The Author(s) 2018. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 7. — Model of H. pullorum N-linked protein glycosylation pathways. Direct evidence for role of PglCAJHB1 and WbpOS is provided in this study. The proposed roles of PglDEFK and PglB2 are based on established function of C. jejuni orthologues. The H. pullorum PglB1-dependent N-linked pentasaccharide glycan is assembled through sequential action of glycosyltransferases PglCAJH, flipped into the periplasm by PglK and transferred to proteins as indicated in the periplasm by PglB1. A second proposed glycan, with a reducing end 228 Da residue synthesized by PglDEF activity, is similarly assembled and flipped into the periplasm where it is transferred to as yet unidentified protein(s) via PglB2 activity.