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. Author manuscript; available in PMC: 2020 Jun 30.
Published in final edited form as: J Proteomics. 2019 May 4;202:103374. doi: 10.1016/j.jprot.2019.05.002

Figure 2.

Figure 2

Analysis of VacA and Omp peptide distribution. H. pylori was grown in high salt conditions (1.25% NaCl for 24 h), and broth culture supernatants were processed as described in Methods. Spectral counts for peptides assigned exclusively to VacA, HomA, or HopQ were analyzed. The x -axis corresponds to the amino acid position for each protein and the y-axis indicates the number of assigned spectra. Regions of VacA corresponding to a signal sequence (SS), p33 domain, p55 domain, and C-terminal β-barrel domain are shown. The C-terminal portions of HomA and HopQ are predicted to have a β-barrel architecture, based on use of the program BOCTOPUS, a transmembrane β-barrel topology prediction tool (http://boctopus.bioinfo.se/)[63].