Identification of boric acid as a novel chemoattractant and elucidation of its chemoreceptor in Ralstonia pseudosolanacearum Ps29

• Published in: Scientific reports Vol. 7; no. 1; pp. 8609 - 10
• Main Authors: Hida, Akiko, Oku, Shota, Nakashimada, Yutaka, Tajima, Takahisa, Kato, Junichi
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 17.08.2017; Nature Publishing Group; Nature Portfolio
• Subjects: 14/63; 45/41; 631/326/1320; 631/326/171/1818; 82/83; Acids; Boric acid; Calorimetry; Chemotactic response; Chemotaxis; Deletion mutant; Environmental conditions; Humanities and Social Sciences; McpB protein; multidisciplinary; pH effects; Preservatives; Science; Science (multidisciplinary); Titration; Ultracentrifugation
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/s41598-017-09176-3

Chemotaxis enables bacteria to move toward more favorable environmental conditions. We observed chemotaxis toward boric acid by Ralstonia pseudosolanacearum Ps29. At higher concentrations, the chemotactic response of R. pseudosolanacearum toward boric acid was comparable to or higher than that toward L-malate, indicating that boric acid is a strong attractant for R. pseudosolanacearum . Chemotaxis assays under different pH conditions suggested that R. pseudosolanacearum recognizes B(OH) 3 (or B(OH 3 ) + B(OH) 4 − ) but not B(OH) 4 − alone. Our previous study revealed that R. pseudosolanacearum Ps29 harbors homologs of all 22 R. pseudosolanacearum GMI1000 mcp genes. Screening of 22 mcp single-deletion mutants identified the RS_RS17100 homolog as the boric acid chemoreceptor, which was designated McpB. The McpB ligand-binding domain (LBD) was purified in order to characterize its binding to boric acid. Using isothermal titration calorimetry, we demonstrated that boric acid binds directly to the McpB LBD with a K D (dissociation constant) of 5.4 µM. Analytical ultracentrifugation studies revealed that the McpB LBD is present as a dimer that recognizes one boric acid molecule.