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The bacterial cytoskeleton is a collective term for a diverse group of protein filaments that serve as structural and functional homologs to eukaryotic actin, tubulin, and intermediate filaments (Schumacher, 2017, PubMed: 28130281). The most prominent members include FtsZ, a tubulin homolog essential for forming the Z-ring during cytokinesis, and MreB, an actin homolog that maintains cell shape by directing cell wall synthesis in non-spherical bacteria (Vollmer, 2006, PubMed: 16438807). These proteins are critical for bacterial viability, growth, and spatial organization, making them attractive targets for the development of next-generation antibiotics (Schaffner-Barbero et al., 2012, PubMed: 22403578). Because bacterial cytoskeletal proteins share very low sequence identity with their human counterparts, they offer a high potential for selectivity and reduced host toxicity (Bean et al., 2009, PubMed: 19719618). Experimental drugs targeting these proteins, such as the FtsZ inhibitor PC190723 and the MreB inhibitor A22, act by disrupting filament polymerization or enzymatic activity, resulting in severe morphological defects and bacterial cell death (Silber et al., 2020, PubMed: 32102170).
Inhibition of protein polymerization and enzymatic activity (GTPase/ATPase) of cytoskeletal components like FtsZ and MreB, leading to the disruption of cell division and structural integrity (Schaffner-Barbero et al., 2012, PubMed: 22403578).
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