Protein disulfide isomerase (PDI) is a member of the thioredoxin (Trx) superfamily with important functions in cellular stability, ion uptake, and cellular differentiation. While PDI has been extensively studied in humans and animals, its role in fungi remains relatively unknown. In this study,
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Protein disulfide isomerase (PDI) is a member of the thioredoxin (Trx) superfamily with important functions in cellular stability, ion uptake, and cellular differentiation. While PDI has been extensively studied in humans and animals, its role in fungi remains relatively unknown. In this study, the biological functions of FgEps1, a disulfide bond isomerase in the fungal pathogen
Fusarium graminearum, were investigated. It was found that
FgEps1 mutation affected nutritional growth, asexual and sexual reproduction, and stress tolerance. Additionally, its deletion resulted in reduced pathogenicity and impaired DON toxin biosynthesis. The involvement of
FgEps1 in host infection was also confirmed, as its expression was detected during the infection period. Further investigation using a yeast signal peptide secretion system and transient expression in
Nicotiana benthamiana showed that
FgEps1 suppressed the immune response of plants and promoted infection. These findings suggest that virulence factor
FgEps1 plays a crucial role in growth, development, virulence, secondary metabolism, and host infection in
F. graminearum.
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