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Involvement of the two L-lactate dehydrogenase in development and pathogenicity in Fusarium graminearum
- Chen, Wenchan, Wei, Lingling, Zhang, Yu, Shi, Dongya, Ren, Weichao, Zhang, Zhihui, Wang, Jin, Shao, Wenyong, Liu, Xiali, Chen, Changjun, Gao, Qingli
- Current genetics 2019 v.65 no.2 pp. 591-605
- Fusarium graminearum, NAD (coenzyme), biosynthesis, carbon, catalytic activity, corn, deoxynivalenol, functional diversity, genes, head blight, homeostasis, lactate dehydrogenase, lactic acid, mutants, pathogenesis, phenotype, plant pathogenic fungi, pyruvic acid, spikelets, spore germination, sporulation, vegetative growth, virulence, wheat
- Lactate dehydrogenase (LDH) widely exists in organisms, which catalyzes the interconversion of pyruvate into lactate with concomitant interconversion of NADH and NAD⁺. In this study, two L-type lactate dehydrogenase genes FgLDHL1 and FgLDHL2 were characterized in an ascomycete fungus Fusarium graminearum, a causal agent of wheat head blight. Both the single-gene deletion mutants of FgLDHL1 or FgLDHL2 exhibited phenotypic defects in vegetative growth, sporulation, spore germination, L-lactate biosynthesis and activity. Additionally, the two L-lactate dehydrogenases were involved in the utilization of carbon sources and maintenance of redox homeostasis during spore germination. Pathogenicity assays showed that ΔFgLDHL1 exhibits reduced virulence on wheat spikelets and on corn stigmas, suggesting that it was indirectly correlated with a reduced level of deoxynivalenol accumulation. These results indicate that FgLDHL1 and FgLDHL2 play multiple roles in the developmental processes and pathogenesis in F. graminearum, and help understand the functional diversity of D-/L-lactate dehydrogenase in phytopathogenic fungi.