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. 2021 Nov 24;6(12):1583–1592. doi: 10.1038/s41564-021-01003-w

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© The Author(s) 2021

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. 1 — a, MS/MS of the GlcNAc–MurNAc–AlaGluOrnGly muropeptide from B. burgdorferi 5A11 cultured in unlabelled (grey) and [1-¹³C]ManNAc (blue), respectively. Fragmentation data confirm the location of the labelled carbon resides in the glycan component and not the stem peptide. b, Monosaccharide analysis of purified peptidoglycan isolated from B. burgdorferi 5A11 and E. coli K-12. Results were compared with reference standards GlcNAc, MurNAc, ManNAc and GalNAc (below). The inset table highlights the molar percentage of MurNAc present in each bacterial sample. c, LC–MS chromatogram of B. burgdorferi 5A11 peptidoglycan. B. burgdorferi peptidoglycan was purified, digested with mutanolysin and analysed by LC–MS. Each peak corresponds to one or more muropeptides of interest; peaks are labelled as red (GlcNAc–MurNAc muropeptides) or blue (HexNAc–GlcNAc–MurNAc muropeptides). Co-eluting peaks can be found in Supplementary Table 2.