Mreb

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MreB is a protein found in bacteria that has been identified as a homologue of actin, as indicated by similarities in tertiary structure and conservation of active site peptide sequence. The conservation of protein structure suggests the common ancestry of the cytoskeletal elements formed by actin and MreB, found in prokaryotes. Indeed, recent studies have found that MreB proteins polymerize to form filaments that are similar to actin microfilaments. MreB controls the width of rod-shaped bacteria, such as Escherichia coli. A mutant E. Also, bacteria that are naturally spherical do not have the gene encoding MreB.

Mreb

Although many prospective antibiotic targets are known, bacterial infections and resistance to antibiotics remain a threat to public health partly because the druggable potentials of most of these targets have yet to be fully tapped for the development of a new generation of therapeutics. The prokaryotic actin homolog MreB is one of the important antibiotic targets that are yet to be significantly exploited. MreB is a bacterial cytoskeleton protein that has been widely studied and is associated with the determination of rod shape as well as important subcellular processes including cell division, chromosome segregation, cell wall morphogenesis, and cell polarity. Notwithstanding that MreB is vital and conserved in most rod-shaped bacteria, no approved antibiotics targeting it are presently available. Here, the status of targeting MreB for the development of antibiotics is concisely summarized. Expressly, the known therapeutic targets and inhibitors of MreB are presented, and the way forward in the search for a new generation of potent inhibitors of MreB briefly discussed. The emergence of antibiotic-resistant bacterial strains White et al. Nonetheless, the full druggable potentials of most bacterial pharmacological targets have yet to be tapped, and it is not surprising that few antibiotics have been released into the drug market in the past several years Conly and Johnston, The bacterial actin-like MreB is a potential therapeutic target Kruse et al. As an ATPase whose primary function involves coordinating bacterial cell wall biosynthesis Figge et al. MreB is a promising drug target because it is conserved and essential in most rod-shaped bacteria Varley and Stewart, ; Costa and Anton, , ; Burger et al.

Direct membrane binding by bacterial actin MreB. Trends Cell Biol.

The bacterial actin homologue, MreB, is required for the maintenance of a rod-shaped cell and has been shown to form spirals that traverse along the longitudinal axis of Bacillus subtilis and Escherichia coli cells. The depletion of MreB in Caulobacter crescentus resulted in lemon-shaped cells that possessed defects in the integrity of the cell wall. MreB localization appeared as bands or spirals that encircled the cell along its entire length and switched to a mid-cell location at a time that coincided with the initiation of cell division. The formation of smaller MreB spirals or bands at the mid-cell was dependent on the presence on the cytokinetic protein, FtsZ. Penicillin-binding protein 2 PBP2 also formed band-like structures perpendicular to the cell periphery that resembled, and depended upon, MreB localization. PBP2 co-immunoprecipitated with several other penicillin-binding proteins, suggesting that these proteins are in association in Caulobacter cells. We hypothesize that MreB filaments function as a cytoskeleton that serves as an organizer or tracking device for the PBP2-peptidoglycan biosynthesis complex.

Federal government websites often end in. The site is secure. MreB, the bacterial actin homologue, plays a vital role in determining cell shape, but the mechanisms by which it actually functions have remained largely mysterious. Recent studies now shed new light on MreB, demonstrating that it associates with many cell-wall synthesis enzymes, including a newly identified family of proteins that mediate teichoic acid synthesis in Gram-positive bacteria. Furthermore, MreB filaments dynamically rotate around the cell circumference in a manner dependent on the cell-wall assembly machinery. Thus, MreB may function to spatially organize the enzymatic activities required for proper bacterial growth see Figure 1. Potential functions of the MreB cytoskeleton in regulating cell shape.

Mreb

Federal government websites often end in. The site is secure. Although many prospective antibiotic targets are known, bacterial infections and resistance to antibiotics remain a threat to public health partly because the druggable potentials of most of these targets have yet to be fully tapped for the development of a new generation of therapeutics.

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Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. USA , — Relative rates of surface and volume synthesis set bacterial cell size. Testing the Membrane Real Estate Hypothesis. To test this, the diffusion of several membrane proteins was followed using high-speed total internal reflection TIRF microscopy. A further truncation RodZ 70— and deletion of the entire helix-turn-helix motif RodZ 83— show a further dampening of the curvature enrichment profile. Shaevitz, J. The staining of B. Background fluorescence was subtracted using signals measured from Nile Red in LB. For a complete list of strains see Supplementary Table 1. It has been shown that this dye exhibits a fluorescent stain in B. Role of the Bacillus subtilis fatty acid desaturase in membrane adaptation during cold shock. Full color palette of fluorescent D-amino acids for in situ labeling of bacterial cell walls. Sceptrin Figure 2G is a natural product isolated from a marine sponge, Agelas confera Walker et al. Actin polymerization serves as a membrane domain switch in model lipid bilayers.

Federal government websites often end in. The site is secure.

Furthermore, while E. Powerful imaging tools for quantifying cell shape and mapping cell growth To understand the spatiotemporal dynamics of cell shape determination, maps of where and when cell-wall growth takes place and which proteins are colocalized there in time and space have be used to reverse engineer the blueprint for cell construction. By altering cell shape, A22 is also able to inhibit the motility, surface adhesion, and biofilm formation properties required for bacterial infections and antibiotic resistance Bonez et al. The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by X-ray crystallography. For other comparisons see Supplementary Table 3. Masuda, H. Lipid-linked cell wall precursors regulate membrane association of bacterial actin MreB. In fact, the delocalization of MreB with CCCP does coincide with a loss of lateral Lipid II localization, based on staining with fluorescently-labelled vancomycin, whereas staining of the cell division septum remains unaffected Supplementary Fig. To prevent rapid adaptation of membrane fluidity 67 , the measurements were carried out with a lipid desaturase des -deficient strain. Article Google Scholar Lucero, H.