Journal
PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY
Volume 184, Issue -, Pages -Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pestbp.2022.105130
Keywords
Penicillium digitatum; Boscalid; Resistance risk; Resistance mechanism; H243Y
Categories
Funding
- China Agriculture Research System of MOF and MARA
- Fundamental Research Funds for the Central Universities [2662020ZKPY018]
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This study evaluated the risk and molecular mechanisms of boscalid resistance in Penicillium digitatum. Mutations in the SdhB subunit were found to play a role in resistance by blocking the binding of boscalid to the quinone-binding site of SDH. The resistant mutants exhibited differences in growth, sporulation, pathogenicity, and sensitivity to external stresses.
The succinate dehydrogenase inhibitor (SDHI) fungicide boscalid is an excellent broad-spectrum fungicide but has not been registered in China to control Penicillium digitatum, the causal agent of green mold of citrus. The present study evaluated the risk and molecular mechanisms for boscalid resistance in P. digitatum. Resistance induction with four arbitrarily selected sensitive isolates of P. digitatum by ultraviolet (UV) irradiation on conidia plated on boscalid-amended potato dextrose agar (PDA) and consecutive growing on boscalid-amended PDA produced five highly resistant isolates with EC50 values greater than 1000 mu g/mL and two resistant isolates with EC50 lower than 200 mu g/mL. Boscalid resistance of the five mutants with EC50 values above 1000 mu g/mL was stable after successive transfers on PDA for 16 generations. However, for the other two mutants with EC50 lower than 200 mu g/mL, the EC50 values decreased significantly after successive transfers. There was significant crossresistance between boscalid and carboxin (r = 0.925, P < 0.001), but no significant cross-resistance was detected between boscalid and fludioxonil (r = 0.533,P = 0.095) or between boscalid and prochloraz (r = 0.543,P = 0.088). The seven resistant mutants varied greatly in the mycelia growth, sporulation, pathogenicity, and sensitivities to exogenous stresses including NaCl, salicylhydroxamic acid (SHAM), and H2O2. Alignment of the deduced amino acid sequence showed that there was no point mutation in the target enzyme succinate dehydrogenase (Sdh) subunits SdhA, SdhC, or SdhD in each of the seven resistant mutants, and the mutation of a conserved histidine residue to tyrosine (H243Y) in the subunit SdhB (i.e., iron-sulfur protein) occurred in only three highly resistant isolates. Molecular docking indicated that mutation H243Y could not prevent the binding of boscalid into the quinone-binding site of SDH in the presence of the heme moiety. However, for SDH without the heme moiety, boscalid could bind into a deeper site with a much higher affinity, and the mutation H243Y spatially blocked the docking of boscalid into the deeper site. This may be the molecular mechanism for boscalid resistance caused by SdhB-H243Y mutation.
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