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. 2019 Aug 27;10:1967. doi: 10.3389/fimmu.2019.01967

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Copyright © 2019 Shathili, Bandala-Sanchez, John, Goddard-Borger, Thaysen-Andersen, Everest-Dass, Adams, Harrison and Packer.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Mapping the O-glycosylation of recombinant human CD52. (A) N- and O-glycan occupancy of CD52 I, CD52 II, and selected MonoQ fractions (F31 and F46–F51) measured at the protein level after de-N-glycosylation. (B) PGC resolution of O-glycosylated isomers from active fractions m/z 665.2²⁻ (GalNAc₁GlcNAc₁Gal₂NeuAc₂) and m/z 1040.4¹⁻ (GalNAc₁GlcNAc₁Gal₂NeuAc₁). (C) EThcD-MS/MS based site localization analysis showing the peptide backbone fragments and the ions diagnostic of the amino acid site for both aforementioned O-glycans. Fragmentation to c and z ions are shown that indicate that (i) di-sialylated O-glycans were conjugated to Ser12, and possibly Ser10, whereas (ii) the mono-sialylated O-glycans are found on Thr8.