Phospholipase C-mediated calcium signalling is required for fungal development and pathogenicity in Magnaporthe oryzae.
Calcium signalling has profound implications in the fungal infection of plants and animals, during which a series of physiological and morphological transitions are required. In this article, using a model fungal pathogen, Magnaporthe oryzae, we demonstrate that the regulation of the intracellular calcium concentration ([Ca(2+)](int)) is essential for fungal development and pathogenesis. Imaging of [Ca(2+)](int) showed that infection-specific morphogenesis is highly correlated with the spatiotemporal regulation of calcium flux. Deletion of the fungal phospholipase C gene (M. oryzae phospholipase C 1, MoPLC1) suppressed calcium flux, resulting in a fungus defective in developmental steps, including appressorium formation and pathogenicity. Surprisingly, the PLC-delta1 gene of mouse was able to functionally substitute for MoPLC1 by restoring the calcium flux, suggesting the evolutionary conservation of the phospholipase C-mediated regulation of calcium flux. Our results reveal that MoPLC1 is a conserved modulator of calcium flux that is essential for the regulation of key steps in fungal development and pathogenesis.
Rho
Hee-Sool
HS
Department of Agricultural Biotechnology, Center for Fungal Pathogenesis, and Center for Fungal Genetic Resources, Seoul National University, Seoul, Korea.
Jeon
Junhyun
J
Lee
Yong-Hwan
YH
D000818:Animals; D020013:Calcium Signaling; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D005800:Genes, Fungal; D005816:Genetic Complementation Test; D042541:Intracellular Space / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D020082:Magnaporthe / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development / Q000472:pathogenicity*; D051379:Mice; D009024:Morphogenesis; D009997:Osmotic Pressure; D010641:Phenotype; D017434:Protein Structure, Tertiary; D013172:Spores, Fungal / Q000166:cytology / Q000201:enzymology / Q000648:ultrastructure; D010738:Type C Phospholipases / Q000737:chemistry / Q000378:metabolism*
D005656:Fungal Proteins; D007527:Isoenzymes; D010738:Type C Phospholipases