Phospholipase C-mediated calcium signalling is required for fungal development and pathogenicity in Magnaporthe oryzae

Mol Plant Pathol. 2009 May;10(3):337-46. doi: 10.1111/j.1364-3703.2009.00536.x.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium Signaling*
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism
  • Genes, Fungal
  • Genetic Complementation Test
  • Intracellular Space / metabolism
  • Isoenzymes / chemistry
  • Isoenzymes / metabolism
  • Magnaporthe / enzymology*
  • Magnaporthe / genetics
  • Magnaporthe / growth & development
  • Magnaporthe / pathogenicity*
  • Mice
  • Morphogenesis
  • Osmotic Pressure
  • Phenotype
  • Protein Structure, Tertiary
  • Spores, Fungal / cytology
  • Spores, Fungal / enzymology
  • Spores, Fungal / ultrastructure
  • Type C Phospholipases / chemistry
  • Type C Phospholipases / metabolism*

Substances

  • Fungal Proteins
  • Isoenzymes
  • Type C Phospholipases