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. 2014 Mar 4;92(2):258–272. doi: 10.1111/mmi.12549

Fig. 1.

Fig. 1

Maf1 is required for flagellin glycosylation.A. Western blot analysis of glycosylated (+pse) and unglycosylated (−pse) FlaA/B using α-FlaA/B(+pse) and α-FlaA/B(−pse) antibodies of whole-cell (WC) preparations and secreted fractions (SN) of A. caviae strains wild-type and maf1 mutant strains. A Coomassie-stained SDS-PAGE gel showing whole-cell preparations and secreted fractions is shown as a loading control. The samples were also probed with α-GroEL as a cell lysis control for secreted fractions and an additional loading control for whole-cell fractions.B. CID tandem mass spectra of the FlaB peptide 146FQVGADANQTIGFSLSQAGGFSISGIAK173. B(i) MS/MS of the triply charged ion m/z 1135.22 that elutes at 96.22 min from wild-type A. caviae. The ion corresponds to the peptide containing two Pse residues. B(ii) MS/MS of the quadruply charged ion m/z 851.66 that elutes at 96.25 min from wild-type A. caviae. The ion corresponds to the peptide containing two Pse residues. B(iii) MS/MS spectra from A. caviae maf1 mutant flagellin. The quadruply charged ion m/z 692.85 which elutes at 74.43 min corresponds to the unglycosylated peptide. S is the potentially modified serine residue.