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Updated: Mar 15, 2026
Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
Published on: February 17, 2017
treA Codifies for a Trehalase with Involvement in Xanthomonas citri subsp. citri Pathogenicity
André Vessoni Alexandrino1, Leandro Seiji Goto1, Maria Teresa Marques Novo-Mansur1
1Laboratório de Bioquímica e Biologia Molecular Aplicada - LBBMA, Departamento de Genética e Evolução, Universidade Federal de São Carlos, São Carlos, SP, Brazil.
Citrus canker bacterium Xanthomonas citri subsp. citri (Xcc) trehalase enzyme activity was studied. Inability to hydrolyze trehalose sugar increased Xcc virulence, suggesting trehalase alleviates bacterial pathogenicity.
Area of Science:
- Plant Pathology
- Bacteriology
- Enzymology
Background:
- Citrus canker, caused by Xanthomonas citri subsp. citri (Xcc), is a significant citrus disease.
- Trehalase, an enzyme hydrolyzing trehalose, has been linked to Xcc pathogenicity.
- Xanthomonas fuscans subsp. aurantifolii-type C (XauC) causes a milder citrus disease.
Purpose of the Study:
- To characterize the structure and kinetics of Xcc trehalase.
- To investigate the role of Xcc trehalase in citrus canker pathogenesis.
- To compare trehalase activity between Xcc and XauC.
Main Methods:
- Recombinant Xcc trehalase expression and characterization (structural and kinetic analysis).
- Gene deletion to create an Xcc trehalase mutant strain (XccΔtreA).
- Enzymatic activity assays on cellular lysates of Xcc, XauC, and XccΔtreA.
- Infection assays on Citrus aurantifolia leaves using wild-type Xcc and XccΔtreA.
Main Results:
- Recombinant Xcc trehalase showed specific secondary structures and Michaelis-Menten kinetics (KM = 0.077 mM, Vmax = 55.308 μMol glucose.min-1.mg protein-1).
- XauC exhibited the highest trehalase activity under in vitro infective conditions; XccΔtreA showed no activity.
- Citrus aurantifolia leaves infected with XccΔtreA displayed increased maceration and necrosis compared to wild-type Xcc infections.
Conclusions:
- Trehalase activity in Xcc contributes to reduced bacterial virulence.
- Impaired trehalose hydrolysis by XccΔtreA enhances its infectivity and pathogenicity.
- The study elucidates a novel mechanism by which trehalase modulates citrus canker disease severity.
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