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. 2008 Apr 21;76(7):2966–2977. doi: 10.1128/IAI.00323-08

FIG. 2.

FIG. 2.

Comparison of B. bronchiseptica, B. pertussis, and B. parapertussishu. (A) Alignment of the intergenic region of batB from B. bronchiseptica strain RB50, B. pertussis strain Tohama I, and B. parapertussishu strain 12822. The stop codon of the upstream ORF is gray. Nucleotide differences from the B. bronchiseptica sequence are in boldface type. The batB translational start sites denoted by the Sanger Institute are different in B. bronchiseptica strain RB50 (red box), B. pertussis strain Tohama I (purple box), and B. parapertussishu strain 12822 (green box). The translational start site denoted for B. parapertussishu most likely is the correct translational start site, since it is predicted to encode a signal sequence. All BatB comparisons in this paper use this as the translational start (green lettering). (B) Comparison of BatB from strains RB50 (Bb), Tohama I (Bp), and 12822 (Bpp). Red lines represent single-amino-acid changes away from the B. bronchiseptica sequence, and blue lines represent amino acid changes that are the same in B. pertussis and B. parapertussishu. The BatB signal sequence is represented in black, the region homologous to IgA proteases is blue, the PL2 domain is light gray, and the β-domain is purple. The inverted arrows indicate the region of the protein that was disrupted by plasmid insertion. The solid line below the sequence indicates the region of the protein used to generate an anti-BatB antibody (α-BatB). (C) WCLs of B. bronchiseptica strain RB50, B. pertussis strain BPSM (a streptomycin-resistant derivative of Tohama I), and B. parapertussishu strain 12822 grown under Bvg+- and Bvg-phase conditions were probed with anti-BatB antibody.