ArticleMolecular plant pathology2019
MoImd4 mediates crosstalk between MoPdeH-cAMP signalling and purine metabolism to govern growth and pathogenicity in Magnaporthe oryzae.
Article in Molecular plant pathology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 13 citations in OpenAlex.
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- Carbonic anhydrases contribute to mitochondrial function, conidial development, and pathogenicity ofApplied and environmental microbiology · 2026Article
- Purine metabolism in plant pathogenic fungi.Frontiers in microbiology · 2024Review
- Development and validation of prognostic index based on purine metabolism genes in patients with bladder cancer.Frontiers in medicine · 2023Article
- Pyridoxine biosynthesis protein MoPdx1 affects the development and pathogenicity ofFrontiers in cellular and infection microbiology · 2023Article
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- Transcriptome Analysis ofPlants (Basel, Switzerland) · 2021Article
- Balancing of the mitotic exit network and cell wall integrity signaling governs the development and pathogenicity in Magnaporthe oryzae.PLoS pathogens · 2021Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
The high-affinity cyclic adenosine monophosphate (cAMP) phosphodiesterase MoPdeH is important not only for cAMP signalling and pathogenicity, but also for cell wall integrity (CWI) maintenance in the rice blast fungus Magnaporthe oryzae. To explore the underlying mechanism, we identified MoImd4 as an inosine-5'-monophosphate dehydrogenase (IMPDH) homologue that interacts with MoPdeH. Targeted deletion of MoIMD4 resulted in reduced de novo purine biosynthesis and growth, as well as attenuated pathogenicity, which were suppressed by exogenous xanthosine monophosphate (XMP). Treatment with mycophenolic acid (MPA), which specifically inhibits MoImd4 activity, resulted in reduced growth and virulence attenuation. Intriguingly, further analysis showed that MoImd4 promotes the phosphodiesterase activity of MoPdeH, thereby decreasing intracellular cAMP levels, and MoPdeH also promotes the IMPDH activity of MoImd4. Our studies revealed the presence of a novel crosstalk between cAMP regulation and purine biosynthesis in M. oryzae, and indicated that such a link is also important in the pathogenesis of M. oryzae.
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