FtsZ: A Novel Target for Tuberculosis Drug Discovery

Title: FtsZ: A Novel Target for Tuberculosis Drug Discovery

Volume: 7 Issue: 5

Author(s): Qing Huang, Peter J. Tonge, Richard A. Slayden, Teruo Kirikae and Iwao Ojima

Affiliation:

Keywords: FtsZ, tubulin, GTPase, homology, GTP hydrolysis, polymerization, dynamics, inhibitor

Abstract: The emergence of multi-drug resistant Mycobacterium tuberculosis (Mtb) strains has made many of the currently available anti-TB drugs ineffective. Accordingly there is a pressing need to identify new drug targets. FtsZ, a bacterial tubulin homologue, is an essential cell division protein that polymerizes in a GTP-dependent manner, forming a highly dynamic cytokinetic ring, designated as the Z ring, at the septum site. Following recruitment of other cell division proteins, the Z ring contracts, resulting in closure of the septum and then formation of two daughter cells. Since inactivation of FtsZ or alteration of FtsZ assembly results in the inhibition of Z ring and septum formation, FtsZ is a very promising target for new antimicrobial drug development. This review describes the function and dynamic behaviors of FtsZ, its homology to tubulin, and recent development of FtsZ inhibitors as potential anti-TB agents.

Cite this article as:

Huang Qing, Tonge J. Peter, Slayden A. Richard, Kirikae Teruo and Ojima Iwao, FtsZ: A Novel Target for Tuberculosis Drug Discovery, Current Topics in Medicinal Chemistry 2007; 7 (5) . https://dx.doi.org/10.2174/156802607780059790