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Mycobacterial FtsZ and inhibitors: a promising target for the anti-tubercular drug development.

Authors :
Shinde Y
Pathan A
Chinnam S
Rathod G
Patil B
Dhangar M
Mathew B
Kim H
Mundada A
Kukreti N
Ahmad I
Patel H
Source :
Molecular diversity [Mol Divers] 2024 Oct; Vol. 28 (5), pp. 3457-3478. Date of Electronic Publication: 2023 Nov 27.
Publication Year :
2024

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.<br />Competing Interests: Declarations. Competing interests: The authors declare no competing interests.<br /> (© 2023. The Author(s), under exclusive licence to Springer Nature Switzerland AG.)

Details

Language :
English
ISSN :
1573-501X
Volume :
28
Issue :
5
Database :
MEDLINE
Journal :
Molecular diversity
Publication Type :
Academic Journal
Accession number :
38010605
Full Text :
https://doi.org/10.1007/s11030-023-10759-8