The Y137H mutation in the cytochrome P450 FgCYP51B protein confers reduced sensitivity to tebuconazole in Fusarium graminearum. Issue 6 (5th March 2018)

• Record Type: Journal Article
• Authors: Qian, Hengwei; Du, Juan; Chi, Mengyu; Sun, Xiaomei; Liang, Wenxing; Huang, Jinguang; Li, Baodu
• Is Part Of: Pest management science. Volume 74:Issue 6(2018)
• Page Start: 1472
• Page End: 1477
• Publication Date: 2018-03-05
• Subjects: Fusarium graminearum -- tebuconazole (TEC) -- resistance -- CYP51B -- site‐directed mutagenesis -- molecular docking; Pests -- Control -- Periodicals; Pesticides -- Periodicals; 632.9
• DOI: 10.1002/ps.4837
• Languages: English
• ISSNs: 1526-498X

Abstract

Abstract: BACKGROUND: Fusarium graminearum is the main pathogen of Fusarium head blight (FHB), a worldwide plant disease and one of the most significant wheat diseases in China. Demethylation inhibitor (DMI) fungicides, such as tebuconazole (TEC), are widely used to control FHB, but long‐term use leads to low efficacy against FHB. Earlier studies showed that DMI resistance is associated with the fungal sterol 14α‐demethylase (cytochrome P450 CYP51 ) gene, and that point mutations in the CYP51 gene are the primary mechanism of resistance to DMI fungicides. The aims of this study were to clarify the molecular mechanisms of resistance to TEC and identify the binding sites on the FgCYP51B protein. RESULTS: Site‐directed mutagenesis was used to change the FgCYP51B gene of wild‐type strain PH‐1 from tyrosine to histidine at residue 137 (Y137H) to generate a mutant transformant, which was confirmed to be resistant to TEC compared with the parental strains. A three‐dimensional FgCYP51B model was constructed, and molecular docking simulation studies were conducted to identify the optimum binding mode with TEC. The wild‐type FgCYP51B protein displayed stronger affinity to TEC than that of the mutated FgCYP51B in the molecular docking analysis. CONCLUSION: These results indicate that a Tyr137 amino acid mutation in the cytochrome P450 FgCYP51B could lead to resistance to TEC and that Y137 forms part of the tebuconazole‐binding pocket. © 2017 Society of Chemical Industry Abstract : This article presents a important amino acid of FgCYP51B, Tyrosine 137. It could lead to resistance to tebuconazole when mutated to histidine and forms part of the TEC binding pocket.