Antibiotic resistance to Mycobacterium tuberculosis is a growing problem. 
Therefore, development of new anti-tuberculosis antibiotics is urgent for the 
control of tuberculosis (TB) infections. FtsZ, the homolog of eukaryotic 
tubulin, is a GTPase that assembles into cytokinetic Z rings essential for cell 
division in prokaryotic cells. FtsZ (filamentous temperature-sensitive protein 
Z) polymerizes in a GTP-dependent manner, and polymerization of FtsZ forms into 
dynamic protofilaments. In this study, we screened 20,000 compounds to identify 
inhibitors of GTPase activity of M. tuberculosis FtsZ. We found that 297F 
inhibited GTPase and polymerization of FtsZ, and reduced the amount of FtsZ 
polymers. Furthermore, 297F has anti-TB activity with low cytotoxicity and shows 
no antibacterial activities toward other Gram-positive or Gram-negative strains. 
In vitro, 297F also induced filamentation in Mycobacterium smegmatis. All 
results suggest that 297F inhibits bacterial proliferation by targeting M. 
tuberculosis FtsZ and it may be useful as a lead compound for developing anti-TB 
agents.