Figure 3

Comparison of FimA protein sequences from A. naeslundii genospecies 1 and 2 and A. odontolyticus with different binding properties. A) Shown are conserved regions between FimA and FimP proteins (black boxes) and regions with high (grey boxes) or low (white boxes) sequence identity between FimA proteins. The low FimA amino acid (a.a.) sequence identity regions (unlined, double and triple lined white boxes) are species-specific due to a high strain-to-strain sequence identity for each species. High FimA sequence identity domains include the N-terminal signal peptide, pilin motif, proline-rich region, E box, and LPXTG motif (motifs are marked and the seven conserved proline-containing domains identified by Yeung and Cisar are numbered). The proline-containing domains 1 and 5 of FimA display only a conserved proline residue, in contrast to FimP, in which the entire seven proline-containing domains are conserved. The FimA proteins from genospecies 1 and 2 and A. odontolyticus contains 32, 33 and 32 amino acid signal peptides and 534, 535 and 535 amino acid proteins, respectively. B) Alignment of the pilin, E-box and LPXTG motifs present in FimA from different strains. Postulated key determinants are in bold [29, 39].