Summary In order to overcome the crisis of antibiotic resistance, there is an urgent need for alternative antibacterial agents that have novel mechanisms of action. FtsZ is an attractive target for antibacterial drug discovery because of its widespread conservation in the bacterial kingdom, its absence in the mitochondria of higher eukaryotes and its known biochemical activity and molecular structure. FtsZ plays an essential role in prokaryotic cell division machinery in which undergoes GTP-dependent polymerization midcell and assembles into the dynamic Z-ring at the site of division. The Z-ring acts to initiate Z-ring contraction to form bacterial daughter cells. Although FtsZ shares structural and functional similarity with eukaryotic tubulin, most of the tubulin/microtubule targeting agents do not affect the dynamic assembly of FtsZ, indicating that FtsZ can be a selective antibacterial target. In this study, we evaluated the immunogenicity in mice of FtsZ protein from Pseudomonas aeruginosa bacterium, which is a well-known opporthunistic human pathogen. We were interested in the degree of affinity and titer dynamics of polyclonal antibodies synthesized against Pseudomonas aeruginosa FtsZ by mice reimmunization and also, in antiFtsZ antibodies reactivity with their specific protein, FtsZ Pseudomonas aeruginosa
