Antibacterial Activity of Alkyl Gallates against Xanthomonas citri subsp.
            <i>citri</i>

Silva, I. C.; Regasini, Luís Octávio; Petrônio, Maicon Segalla; Silva, D. H. S.; Bolzani, Vanderlan S.; Belasque, José; Sacramento, Luís Vitor Silva do; Ferreira, Henrique

doi:10.1128/jb.01442-12

Cited by 67 publications

(130 citation statements)

References 46 publications

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“…Here, we further characterized the Xac mutant strain used by Silva et al. () that is labeled for the centromere (Xac parB ::pAPU3), and extended the studies with ParB encoded by this plant pathogen. First, we showed that Xac ParB is stably expressed and operates on chromosome segregation.…”

Section: Discussionmentioning

confidence: 89%

Asymmetric chromosome segregation in Xanthomonas citri ssp. citri

et al. 2013

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This study was intended to characterize the chromosome segregation process of Xanthomonas citri ssp. citri (Xac) by investigating the functionality of the ParB factor encoded on its chromosome, and its requirement for cell viability and virulence. Using TAP tagging we show that ParB is expressed in Xac. Disruption of parB increased the cell doubling time and precluded the ability of Xac to colonize the host citrus. Moreover, Xac mutant cells expressing only truncated forms of ParB exhibited the classical phenotype of aberrant chromosome organization, and seemed affected in cell division judged by their reduced growth rate and the propensity to form filaments. The ParB-GFP localization pattern in Xac was suggestive of an asymmetric mode of replicon partitioning, which together with the filamentation phenotype support the idea that Xac may control septum placement using mechanisms probably analogous to Caulobacter crescentus, and perhaps Vibrio cholerae, and Corynebacterium glutamicum. Xac exhibits asymmetric chromosome segregation, and the perturbation of this process leads to an inability to colonize the host plant.

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Section: Discussionmentioning

confidence: 89%

Asymmetric chromosome segregation in Xanthomonas citri ssp. citri

et al. 2013

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“…The antibacterial activity of the compounds was evaluated using the Resazurin Microtiter Assay Plate (REMA) adapted to X. citri (Silva et al., ). Compounds, as dried powders, were diluted in 100% DMSO to a starting concentration of 10 mg/mL.…”

Section: Methodsmentioning

confidence: 99%

A simplified curcumin targets the membrane of Bacillus subtilis

et al. 2018

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Curcumin is the main constituent of turmeric, a seasoning popularized around the world with Indian cuisine. Among the benefits attributed to curcumin are anti-inflammatory, antimicrobial, antitumoral, and chemopreventive effects. Besides, curcumin inhibits the growth of the gram-positive bacterium Bacillus subtilis. The anti-B. subtilis action happens by interference with the division protein FtsZ, an ancestral tubulin widespread in Bacteria. FtsZ forms protofilaments in a GTP-dependent manner, with the concomitant recruitment of essential factors to operate cell division. By stimulating the GTPase activity of FtsZ, curcumin destabilizes its function. Recently, curcumin was shown to promote membrane permeabilization in B. subtilis. Here, we used molecular simplification to dissect the functionalities of curcumin. A simplified form, in which a monocarbonyl group substituted the β-diketone moiety, showed antibacterial action against gram-positive and gram-negative bacteria of clinical interest. The simplified curcumin also disrupted the divisional septum of B. subtilis; however, subsequent biochemical analysis did not support a direct action on FtsZ. Our results suggest that the simplified curcumin exerted its function mainly through membrane permeabilization, with disruption of the membrane potential necessary for FtsZ intra-cellular localization. Finally, we show here experimental evidence for the requirement of the β-diketone group of curcumin for its interaction with FtsZ.

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“…The nisin, nisin variants, and other lantibiotics used in this study all displayed antibacterial activity against B. subtilis (Table 1), as determined using the resazurin microplate assay (REMA), which uses the resazurin-resorufin dye pair to assess the metabolic capacity of cells (15) (see the methods in the supplemental material). The MIC 50 s determined correspond well with MIC values reported in the literature for the various compounds (8,(16)(17)(18).…”

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confidence: 99%

In Vivo Cluster Formation of Nisin and Lipid II Is Correlated with Membrane Depolarization

Tol

Angeles

Scheffers

2015

Antimicrob Agents Chemother

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Nisin and related lantibiotics kill bacteria by pore formation or by sequestering lipid II. Some lantibiotics sequester lipid II into clusters, which were suggested to kill cells through delocalized peptidoglycan synthesis. Here, we show that cluster formation is always concomitant with (i) membrane pore formation and (ii) membrane depolarization. Nisin variants that cluster lipid II kill L-form bacteria with similar efficiency, suggesting that delocalization of peptidoglycan synthesis is not the primary killing mechanism of these lantibiotics. Lantibiotics form a class of antimicrobial peptides that contain thioether rings formed by lanthionine residues. Nisin, the most studied lantibiotic, is a 34-residue peptide produced by Lactococcus species with antimicrobial activity against a wide range of Grampositive bacteria (see Fig. S1 in the supplemental material). Nisin targets lipid II, the precursor molecule for peptidoglycan (PG) synthesis (1), and kills via two modes of action: (i) formation of large membrane pores and (ii) interference with PG synthesis.Two lanthionine rings in nisin (A and B) form a pyrophosphatebinding cage that binds lipid II and is highly conserved among lipid II-binding lantibiotics (2). The C terminus of nisin is important for membrane integration (3, 4). Nisin-lipid II complexes (8:4 stoichiometry) form pores in the membrane (5-7) that result in the efflux of small molecules and influx of sodium ions, which will lead to cell death. Mutations in the hinge region of nisin either block or severely inhibit pore formation activity, presumably by preventing the hinge region (residues N20, M21, and K22) (see Fig. S1 in the supplemental material) from flipping the C-terminal tail into and across the membrane. Mutants PP-nisin (N20P M21P) and ⌬⌬-nisin (⌬N20 ⌬M21) fail to form pores in liposome efflux assays (7,8). Nisin 1-22 (⌬23-34) cannot dissipate the membrane potential of sensitive Lactococcus species (9). Similar to nisin 1-22, mutacin 1140 and mersacidin bind lipid II but are too short to span the membrane (6, 10). Mutants that do not efficiently form pores are thought to act by affecting cell wall synthesis only.Two mechanisms for lantibiotic interference with PG synthesis are proposed: "occlusion" and "clustering." Occlusion is the binding to the pyrophosphate moiety of lipid II, which blocks incorporation of lipid II into glycan strands (11). Clustering is the formation of nonphysiological domains containing lipid II and nisin in the membrane, which results in delocalized PG synthesis (12).Recently, we used PP-nisin as a tool to cluster lipid II into domains to determine the effect of delocalized lipid II on the localization of proteins involved in PG synthesis (13). PP-nisin was expected not to affect the membrane potential of live cells (7); however, we found that PP-nisin induced membrane potential loss (13). This compromised the localization of many membraneassociated proteins, including MreB (14). Here, we further investigated the effects of various nisin mutants on lipid II clust...

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Antibacterial Activity of Alkyl Gallates against Xanthomonas citri subsp. citri

Cited by 67 publications

References 46 publications

Asymmetric chromosome segregation in Xanthomonas citri ssp. citri

Asymmetric chromosome segregation in Xanthomonas citri ssp. citri

A simplified curcumin targets the membrane of Bacillus subtilis

In Vivo Cluster Formation of Nisin and Lipid II Is Correlated with Membrane Depolarization

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