title: Antifungal activity of plant and bacterial ureases.
abstract: Ureases (EC 3.5.1.5) are nickel-dependent metalloenzymes that catalyze the hydrolysis of urea to ammonia and carbon dioxide. Produced by plants, fungi and bacteria, but not by animals, ureases share significant homology and similar mechanisms of catalysis, although differing in quaternary structures. While fungal and plant ureases are homo-oligomeric proteins of 90 kDa subunits, bacterial ureases are multimers of two (e.g. Helicobacter pylori) or three subunit complexes. It has been proposed that in plants these enzymes are involved in nitrogen bioavailability and in protection against pathogens. Previous studies by our group have shown that plant ureases, but not a bacterial (Bacillus pasteurii) urease, display insecticidal activity. Herein we demonstrate that (Glycine max) embryo-specific soybean urease, jackbean (Canavalia ensiformis) major urease and a recombinant H. pylori urease impair growth of selected phytopathogenic fungi at sub-micromolar concentrations. This antifungal property of ureases is not affected by treatment of the proteins with an irreversible inhibitor of the ureolytic activity. Scanning electron microscopy of urease-treated fungi suggests plasmolysis and cell wall injuries. Altogether, our data indicate that ureases probably contribute to the plant arsenal of defense compounds against predators and phytopathogens and that the urease defense mechanism is independent of ammonia release from urea.
authors.affiliation: Graduate Program in Molecular and Cellular Biology, Center of Biotechnology, Universidade Federal do Rio Grande do Sul-UFRGS, Brazil.
authors.forename: A B
authors.initials: AB
authors.lastname: Becker-Ritt
authors.forename: A H S
authors.initials: AH
authors.lastname: Martinelli
authors.forename: S
authors.initials: S
authors.lastname: Mitidieri
authors.forename: V
authors.initials: V
authors.lastname: Feder
authors.forename: G E
authors.initials: GE
authors.lastname: Wassermann
authors.forename: L
authors.initials: L
authors.lastname: Santi
authors.forename: M H
authors.initials: MH
authors.lastname: Vainstein
authors.forename: J T A
authors.initials: JT
authors.lastname: Oliveira
authors.forename: L M
authors.initials: LM
authors.lastname: Fiuza
authors.forename: G
authors.initials: G
authors.lastname: Pasquali
authors.forename: C R
authors.initials: CR
authors.lastname: Carlini
mesh_terms: D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000378:metabolism / Q000494:pharmacology; D032449:Canavalia / Q000201:enzymology*; D004305:Dose-Response Relationship, Drug; D005658:Fungi / Q000187:drug effects / Q000648:ultrastructure; D016480:Helicobacter pylori / Q000201:enzymology*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000378:metabolism / Q000494:pharmacology; D011994:Recombinant Proteins; D013025:Glycine max / Q000201:enzymology*; D013997:Time Factors; D014510:Urease / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*