AI Article Synopsis

  • Multidrug-resistant tuberculosis (MDR-TB) strains have made many existing anti-TB drugs ineffective, creating a need for new treatment options.
  • The Filament Forming Temperature Sensitive Gene Z (FtsZ) is crucial for cell division in Mycobacterium tuberculosis (Mtb) by forming a key structure that coordinates cell division; when disrupted, the bacteria cannot divide properly.
  • This review highlights FtsZ as a promising target for new anti-tuberculosis drugs and discusses its role in Mtb cell division and the potential of various inhibitors that could impede its function to treat tuberculosis more effectively.

Article Abstract

The emergence of multidrug-resistant tuberculosis (MDR-TB) strains has rendered many anti-TB drugs ineffective. Consequently, there is an urgent need to identify new drug targets against Mycobacterium tuberculosis (Mtb). Filament Forming Temperature Sensitive Gene Z (FtsZ), a member of the cytoskeletal protein family, plays a vital role in cell division by forming a cytokinetic ring at the cell's center and coordinating the division machinery. When FtsZ is depleted, cells are unable to divide and instead elongate into filamentous structures that eventually undergo lysis. Since the inactivation of FtsZ or alterations in its assembly impede the formation of the Z-ring and septum, FtsZ shows promise as a target for the development of anti-mycobacterial drugs. This review not only discusses the potential role of FtsZ as a promising pharmacological target for anti-tuberculosis therapies but also explores the structural and functional aspects of the mycobacterial protein FtsZ in cell division. Additionally, it reviews various inhibitors of Mtb FtsZ. By understanding the importance of FtsZ in cell division, researchers can explore strategies to disrupt its function, impeding the growth and proliferation of Mtb. Furthermore, the investigation of different inhibitors that target Mtb FtsZ expands the potential for developing effective treatments against tuberculosis.

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Source
http://dx.doi.org/10.1007/s11030-023-10759-8DOI Listing

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