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. 2020 Jun 17;11:1191. doi: 10.3389/fmicb.2020.01191

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Copyright © 2020 Duma, Nothaft, Weaver, Fodor, Beadle, Linton, Benoit, Scott, Maier and Szymanski.

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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Mass-spectrometric analysis of Cff WT, pglJ-, and pglX- glycopeptides. Fragmentation of characteristic ions obtained by precursor ion scanning of digested Cff lysate samples using liquid chromatography-mass spectrometry. Red lettering indicates possible glycosylation site. Spectra of WT Cff have two glycans: (A) HexNAc₅-diNAcBac and (B) HexNAc-[Hex]-HexNAc₃-diNAcBac. (C) The peptide from the pglJ- mutant only shows the presence of a mass consistent with HexNAc-diNAcBac. (D) The peptide from the pglX- mutant indicates that it is modified with HexNAc-HexNac-diNAcBac.