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. Author manuscript; available in PMC: 2021 May 2.
Published in final edited form as: Nat Microbiol. 2020 Nov 2;6(1):19–26. doi: 10.1038/s41564-020-00798-4

Extended Data Fig. 2. Automated spectrum assignment identifies PG modifications on C. burnetii OM proteins.

Extended Data Fig. 2

Representative MS/MS spectra for C. burnetii BbpA, ala-BbpA, BbpB β-barrel proteins and the lipoprotein LimB, covalently attached to mDAP (m) residues of PG. Spectra are shown as annotated by Byonic with manual annotations corresponding to internal fragments in black. J[+72.0848] has been replaced by m to represent mDAP. The PG tripeptide (AEm) is highlighted in red in the HCD spectra showing covalent attachment of PG to BbpA, ala-BbpA, and BbpB. The LimB Lys21 residue with PG tripeptide modification is highlighted in red in the ETD spectra showing covalent attachment of PG to LimB.