The ER chaperone LHS1 is involved in asexual development and rice infection by the blast fungus magnaporthe oryzae

Mihwa Yi, Myoung Hwan Chi, Chang Hyun Khang, Sook Young Park, Seogchan Kang, Barbara Valent, Yong Hwan Lee

Research output: Contribution to journalArticlepeer-review

78 Scopus citations

Abstract

In planta secretion of fungal pathogen proteins, including effectors destined for the plant cell cytoplasm, is critical for disease progression. However, little is known about the endoplasmic reticulum (ER) secretion mechanisms used by these pathogens. To determine if normal ER function is crucial for fungal pathogenicity, Magnaporthe oryzae genes encoding proteins homologous to yeast Lhsip and Kar2p, members of the heat shock protein 70 family in Saccharomyces cerevisiae, were cloned and characterized. Like their yeast counterparts, both LHS1 and KAR2 proteins localized in the ER and functioned in an unfolded protein response (UPR) similarto the yeast UPR. Mutants produced by disruption oiLHSI were viable but showed a defect in the translocation of proteins across the ER membrane and reduced activities of extracellular enzymes. The Δlhs1 mutant was severely impaired not only in conidiation, but also in both penetration and biotrophic invasion in susceptible rice (Oryza sativa) plants. This mutant also had defects in the induction of the Pi-ta resistance gene-mediated hypersensitive response and in the accumulation of fluorescently-labeled secreted effector proteins in biotrophic interfacial complexes. Our results suggest that proper processing of secreted proteins, including effectors, by chaperones in the ER is requisite for successful disease development and for determining host-pathogen compatibility via the gene-for-gene interaction.

Original languageEnglish (US)
Pages (from-to)681-695
Number of pages15
JournalPlant Cell
Volume21
Issue number2
DOIs
StatePublished - Feb 2009

All Science Journal Classification (ASJC) codes

  • Plant Science
  • Cell Biology

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