4.7 Article

SDH mutations confer complex cross-resistance patterns to SDHIs in Corynespora cassiicola

Journal

PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY
Volume 186, Issue -, Pages -

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pestbp.2022.105157

Keywords

Corynespora cassiicola; Succinate dehydrogenase inhibitors; Resistance monitoring; Binding features

Funding

  1. Modern Agricultural Industry Technology System for Vegetables in Shandong Province [SDAIT-05]
  2. National Natural Science Foundation of China [32001953]

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This study reveals the variation in sensitivity of Corynespora cassiicola, the causal agent of Corynespora leaf spot, to succinate dehydrogenase inhibitors (SDHIs). Amino acid mutations in the sdhB/C/D genes of resistant strains affect the activity and binding features of SDH, resulting in multiple resistance levels and complex cross-resistance patterns to different SDHIs. This research provides a significant foundation for the development of efficient chemical control and integrated management strategies for Corynespora leaf spot.
Succinate dehydrogenase inhibitors (SDHIs) are one of the most frequently used fungicides in cucumber fields in China. Our previous studies indicated that the sensitivity profile of Corynespora cassiicola, the causal agent of Corynespora leaf spot, to different SDHIs varied greatly; however, the underlying mechanism remains unclear. The 50% effective concentration (EC50) values of boscalid, fluopyram, fluxapyroxad and isopyrazam in C. cassiicola collected from 2017 to 2020 shifted, with resistance frequencies of 79.83%, 78.43%, 83.19% and 49.86%, respectively. The sequence alignment of sdhB/C/D of resistant strains revealed that eight single amino acid mutations (B-H278Y/L, B-I280V, C-S73P, C-N75S, C-H134R, D-D95E and D-G109V), and three dualmutations (B-I280V&C-S73P, B-I280V&C-N75S and C-S73P&C-N75S) conferred various SDHI resistance levels and cross-resistance profiles. The expression level of the sdhB/C/D gene and succinate dehydrogenase (SDH) activity in the mutants were significantly altered by the presence of SDHIs, compared with the wild type strain. Additionally, molecular docking results suggested that the missense mutation influenced the crystal structure of SDH and subsequently interfered with the interaction bonds and bond distances among the target protein and chemicals. In brief, amino acid mutations altered the fungicide response of target gene expression, SDH activity and the binding features of SDH-ligand complexes and subsequently conferred multiple resistance levels and complex cross-resistance patterns to SDHIs in C. cassiicola. The evaluation of C. cassiicola resistance to SDHIs provided a significant foundation for efficient chemical development and integrated CLS management strategies.

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