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Open AccessJournal ArticleDOI

The Emerging Role of Urease as a General Microbial Virulence Factor

Julian C. Rutherford
- 15 May 2014 - 
- Vol. 10, Iss: 5, pp 0-0
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TLDR
The role of Urease in the virulence of some bacterial pathogens is well established; however, more recent studies are beginning to highlight the function of urease during human fungal infections, suggesting that this enzyme has a wide role during microbial infection.
Abstract
Urea is generated in humans following the breakdown of amino acids and is evenly distributed throughout the body, including in the central nervous system, subcutaneous adipose tissue, blood serum, and epithelial lining fluid [1], [2]. Various pathogenic microbes are able to utilise urea as a nitrogen source through the activity of the enzyme urease that converts urea into ammonia and carbamic acid, with the spontaneous hydrolysis of carbamic acid to carbonic acid generating a further ammonia molecule. CH4N2O+H2O→NH3+CH3NO2 CH3NO2+H2O→NH3+H2CO3 Under physiological conditions the proton of carbonic acid dissociates, and the ammonia molecules become protonated to form ammonium, causing an increase in local pH that can interfere with host function. The role of urease in the virulence of some bacterial pathogens is well established; however, more recent studies are beginning to highlight the function of urease during human fungal infections, suggesting that this enzyme has a wide role during microbial infection.

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Plant Natural Products Targeting Bacterial Virulence Factors

TL;DR: This review presents an updated discussion of natural compounds isolated from plants with chemically characterized structures and activity against the major bacterial virulence factors: quorum sensing, bacterial biofilms, bacterial motility, bacterial toxins, bacterial pigments, bacterial enzymes, and bacterial surfactants.
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Transition Metal Sequestration by the Host-Defense Protein Calprotectin

TL;DR: Recent studies of the coordination chemistry of Calprotectin highlight studies of its metal-binding properties and contributions to the metal-withholding innate immune response and provide a foundation for further investigations of a remarkable metal-chelating protein at the host-microbe interface and beyond.
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Ureases: Historical aspects, catalytic, and non-catalytic properties - A review.

TL;DR: Urease (urea amidohydrolase, EC 3.5) is a nickel-containing enzyme produced by plants, fungi, and bacteria that catalyzes the hydrolysis of urea into ammonia and carbamate as discussed by the authors.
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Survival of Helicobacter pylori in gastric acidic territory.

TL;DR: Helicobacter pylori is well adapted to colonize the epithelial surface of the human gastric mucosa and can cause persistent infections.
References
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Journal ArticleDOI

Alternative activation of macrophages

TL;DR: The evidence in favour of alternative macrophage activation by the TH2-type cytokines interleukin-4 (IL-4) and IL-13 is assessed, and its limits and relevance to a range of immune and inflammatory conditions are defined.
Journal ArticleDOI

A H+-Gated Urea Channel: The Link Between Helicobacter pylori Urease and Gastric Colonization

TL;DR: UreI is an inner membrane protein with six transmembrane segments as shown by in vitro transcription/translation and membrane separation Expression of ureI in Xenopus oocytes results in acid-stimulated urea uptake, with a pH profile similar to activation of cytoplasmic urease as discussed by the authors.
Journal Article

Urease. The primary cause of infection-induced urinary stones.

TL;DR: In this article, it was shown that bacterial urease alkalinizes urine, thereby causing: (i) supersaturation with respect to struvite and calcium phosphate; and (ii) formation of struveite and apatite crystals.
Journal ArticleDOI

Urease as a virulence factor in experimental cryptococcosis.

TL;DR: The results suggest that urease activity is involved in the pathogenesis of cryptococcosis but that the importance may be species and/or infection site specific.
Related Papers (5)
Trending Questions (2)
How is urease activity regulated in the human body?

Urease activity in the human body is regulated by converting urea into ammonia and carbamic acid, leading to ammonia secretion that increases local pH, interfering with host function during microbial infections.

Does the body produce urease?

The paper does not explicitly mention whether the body produces urease.