Fusarium head blight (FHB) caused by
Fusarium graminearum is a significant disease among cereal crops. In
F. graminearum, biosynthesis of leucine, which is a branched chain amino acid, is achieved by converting α-isopropylmalate to β-isopropylmalate catalyzed by isopropylmalate isomerase encoded by
LEU1
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Fusarium head blight (FHB) caused by
Fusarium graminearum is a significant disease among cereal crops. In
F. graminearum, biosynthesis of leucine, which is a branched chain amino acid, is achieved by converting α-isopropylmalate to β-isopropylmalate catalyzed by isopropylmalate isomerase encoded by
LEU1. Considering the potential for targeting this pathway by fungicides, we characterized the gene
FgLEU1 (FGSG-09589) in the
Fusarium graminearum genome using bioinformatics methods. For functional characterization, we constructed a deletion mutant of
FgLEU1 (Δ
LEU1) through homologous recombination. Compared with the wild-type strain PH-1, Δ
LEU1 showed slower colony growth and fewer aerial mycelia. Leucine addition was needed to ensure proper mutant growth. Further, Δ
LEU1 showed decreased conidial production and germination rates, and could not produce ascospores. Moreover, Δ
LEU1 showed complete loss of pathogenicity and reduced ability to produce deoxynivalenol (DON) and aurofusarin. Upstream and downstream genes of
FgLEU1 were significantly upregulated in Δ
LEU1. Contrary to previous reports, the deletion mutant was more resistant to osmotic stress and cell wall-damaging agents than the wild-type. Taken together, FgLEU1 plays a crucial role in leucine synthesis, aerial mycelial growth, sexual and asexual reproduction, pathogenicity, virulence, and pigmentation in
Fusarium graminearum, indicating its potential as a target for novel antifungal agents.
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