Antifungal activity of plant and bacterial ureases

Becker-Ritt, Arlete Beatriz; Martinelli, Anne Helene Souza; Mitidieri, Sydnei; Feder, Vanessa; Wassermann, German Enrique; Santi, Lucélia; Vainstein, Marilene Henning; Oliveira, José T.A.; Fiúza, Lidia Mariana; Pasquali, Giancarlo; Carlini, Célia R.

doi:10.1016/j.toxicon.2007.07.008

Cited by 77 publications

(63 citation statements)

References 61 publications

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“…In plants, ureases are involved in the metabolism of urea arising from different metabolic pathways (Polacco and Holland 1993). This protein may also play other important roles unrelated to its enzyme activity (Carlini and Polacco 2008), including insecticidal (Follmer et al 2004;Staniscuaski et al 2005), fungicidal (Becker-Ritt et al 2007) and exocytosis-inducing properties (Barja-Fidalgo et al 1991). In microorganisms, urease enables the utilization of urea as a nitrogen source and, in some cases, contributes as a virulence factor to several human and animals diseases, such as gastroduodenal infection by Helicobacter pylori and urinary stone formation by Proteus mirabilis (Mulrooney and Hausinger 2003).…”

Section: Introductionmentioning

confidence: 99%

Biochemical and structural studies on native and recombinant Glycine max UreG: a detailed characterization of a plant urease accessory protein

et al. 2012

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Urea is the nitrogen fertilizer most utilized in crop production worldwide. Understanding all factors involved in urea metabolism in plants is an essential step towards assessing and possibly improving the use of urea by plants. Urease, the enzyme responsible for urea hydrolysis, and its accessory proteins, necessary for nickel incorporation into the enzyme active site and concomitant activation, have been extensively characterized in bacteria. In contrast, little is known about their plant counterparts. This work reports a detailed characterization of Glycine max UreG (GmUreG), a urease accessory protein. Two forms of native GmUreG, purified from seeds, were separated by metal affinity chromatography, and their properties (GTPase activity in absence and presence of Ni(2+) or Zn(2+), secondary structure and metal content) were compared with the recombinant protein produced in Escherichia coli. The binding affinity of recombinant GmUreG (rGmUreG) for Ni(2+) and Zn(2+) was determined by isothermal titration calorimetry. rGmUreG binds Zn(2+) or Ni(2+) differently, presenting a very tight binding site for Zn(2+) (K (d) = 0.02 ± 0.01 μM) but not for Ni(2+), thus suggesting that Zn(2+) may play a role on the plant urease assembly process, as suggested for bacteria. Size exclusion chromatography showed that Zn(2+) stabilizes a dimeric form of the rGmUreG, while NMR measurements indicate that rGmUreG belongs to the class of intrinsically disordered proteins. A homology model for the fully folded GmUreG was built and compared to bacterial UreG models, and the possible sites of interaction with other accessory proteins were investigated.

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Section: Introductionmentioning

confidence: 99%

Biochemical and structural studies on native and recombinant Glycine max UreG: a detailed characterization of a plant urease accessory protein

et al. 2012

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“…6,15 Both bacterial and plant ureases display several biological activities that are independent of their ureolytic activity. [16][17][18][19][20] For example, enzymatic activity is not involved in platelet aggregation and antifungal activities of plant and microbial ureases. 17,19,20 Similarly, the lethal activity of canatoxin (an isoform of JBU) in mice and the insecticidal activity of plant ureases are independent of ureolytic activity.…”

mentioning

confidence: 99%

“…[16][17][18][19][20] For example, enzymatic activity is not involved in platelet aggregation and antifungal activities of plant and microbial ureases. 17,19,20 Similarly, the lethal activity of canatoxin (an isoform of JBU) in mice and the insecticidal activity of plant ureases are independent of ureolytic activity. 16,17 It is interesting to note that, in spite of their closely related amino acid sequences, the insecticidal activity of ureases differ significantly among plant and bacterial ureases.…”

mentioning

confidence: 99%

Crystal Structure of the First Plant Urease from Jack Bean: 83 Years of Journey from Its First Crystal to Molecular Structure

Balasubramanian

Ponnuraj

2010

Journal of Molecular Biology

285

205

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“…Such morphological features of bacterial cells may be caused by the lysis of the outer membrane, followed by the loss of electron-dense materials on the surface. The loss of electron dense material from the cells treated with naringenin indicates a loss of cell constituents and a breakdown of the cell walls, resulting in the facilitated release of inner-cell material [34,35]. Morphological analyses of freshwater cyanobacteria treated with naringenin exhibited higher amounts exopolysaccharides than were observed in the halophilic strains.…”

Section: Resultsmentioning

confidence: 99%

Modulation of the growth and metabolic response of cyanobacteria by the multifaceted activity of naringenin

2017

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The interactions between the plant-derived bioflavonoid, naringenin, and prokaryotic microalgae representatives (cyanobacteria), were investigated with respect to its influence on the growth and metabolic response of these microorganisms. To achieve reliable results, the growth of cyanobacteria was determined based on measurements of chlorophyll content, morphological changes were assessed through microscopic observations, and the chemical response of cells was determined using liquid and gas chromatography (HPLC; GC-FID). The results show that micromolar levels of naringenin stimulated the growth of cyanobacteria. Increased growth was observed for halophilic strains at naringenin concentrations below 40 mg L-1, and in freshwater strains at concentrations below 20 mg L-1. The most remarkable stimulation was observed for the freshwater species Nostoc muscorum, which had a growth rate that was up to 60% higher than in the control. When naringenin was examined at concentrations above 40 mg L-1, the growth of the tested microorganisms was inhibited. Simultaneously, an intensive excretion of exopolysaccharides was observed. Microscopic observations strongly suggest that these effects resulted from a structural disturbance of cyanobacterial cell walls that was exerted by naringenin. This phenomenon, in combination with the absorption of naringenin into cell wall structures, influenced cell permeability and thus the growth of bacteria. Fortunately, almost all the naringenin added to the culture was incorporated into to cell substructures and could be recovered through extraction, raising the possibility that this modulator could be recycled.

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Antifungal activity of plant and bacterial ureases

Cited by 77 publications

References 61 publications

Biochemical and structural studies on native and recombinant Glycine max UreG: a detailed characterization of a plant urease accessory protein

Biochemical and structural studies on native and recombinant Glycine max UreG: a detailed characterization of a plant urease accessory protein

Crystal Structure of the First Plant Urease from Jack Bean: 83 Years of Journey from Its First Crystal to Molecular Structure

Modulation of the growth and metabolic response of cyanobacteria by the multifaceted activity of naringenin

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