Fig. 1
From: Characterization of the inner membrane protein BB0173 from Borrelia burgdorferi
Organization and conservation of bb0173. a Schematic demonstrating the similarity between the Bat region of Borrelia burgdorferi (BB), Borrelia hermsii (BH), Leptospira interrogans (LB), Leptospira biflexa (LBF), and Bacteroides fragilis (BF). Note the similarities across BB0172 through BB0176. b Map demonstrating the pertinent domains of BB0173. The map demonstrates the three transmembrane domains (amino acids: 7–25, 57–77, 310–328), VWFA domain (amino acids: 87–328), MIDAS motif (amino acids: 99–103), BatA domain (amino acids: 9–86), and N-glycosylation sites (amino acids 170–172, 265–267). Additionally, a 30-mer peptide is denoted, BB0173pep, which was used to generate chicken anti-BB0173 antibodies. BB0173T, the truncated BB0173 protein, was also used to generate chicken anti-BB0173 antibodies. c Clustal W (v1.83) alignment of B. burgdorferi B31 BB0173 (bold) against homologues in B. burgdorferi ZS7 (BB0173 BbZS7) Borrelia garinii (BG0172), Borrelia afzelii (BAPKO_0175), and the relapsing fever species Borrelia hermsii (BH0173) and Borrelia turicatae (BT0173). Alignments are also made to B. burgdorferi B31 BB0172 (BB0172 B31), which was found to be very similar in sequence and topology. There is also homology seen to Plasmodium falciparum membrane protein TRAP (Pf TRAP) as well as to the human adhesins LFA-1 (hLFA-1) and CD11b (hCD11b). Conserved residues corresponding to the MIDAS motif are highlighted, including the DXSXS as well as the threonine (T) required for MIDAS function