OPEN ACCESS ARTICLE

This Article Free via Open Access: OA OA Full Text Full Text (PDF) Supplemental Data Author Profile OA All Versions of this Article: 21/2/681    most recent tpc.107.055988v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in Plant Cell Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Yi, M. Articles by Lee, Y.-H. Search for Related Content PubMed PubMed Citation Articles by Yi, M. Articles by Lee, Y.-H. Agricola Articles by Yi, M. Articles by Lee, Y.-H.

The ER Chaperone LHS1 Is Involved in Asexual Development and Rice Infection by the Blast Fungus Magnaporthe oryzae^[C],[W],[OA]

^a Department of Agricultural Biotechnology, Center for Fungal Genetic Resources and Center for Fungal Pathogenesis, Seoul National University, Seoul 151-921, Korea
^b Department of Plant Pathology, Kansas State University, Manhattan, Kansas 66506
^c Department of Plant Pathology, Pennsylvania State University, University Park, Pennsylvania 16802

² Address correspondence to yonglee{at}snu.ac.kr.

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 Lhs1p 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) similar to the yeast UPR. Mutants produced by disruption of LHS1 were viable but showed a defect in the translocation of proteins across the ER membrane and reduced activities of extracellular enzymes. The lhs1 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.

Related articles in Plant Cell:

Functional ER Chaperone Required in Rice Blast Disease

Gregory Bertoni
Plant Cell 2009 21: 366. [Full Text]  

This article has been cited by other articles:

				G. Mosquera, M. C. Giraldo, C. H. Khang, S. Coughlan, and B. Valent Interaction Transcriptome Analysis Identifies Magnaporthe oryzae BAS1-4 as Biotrophy-Associated Secreted Proteins in Rice Blast Disease PLANT CELL, April 1, 2009; 21(4): 1273 - 1290. [Abstract] [Full Text] [PDF]

				G. Bertoni Functional ER Chaperone Required in Rice Blast Disease PLANT CELL, February 1, 2009; 21(2): 366 - 366. [Full Text] [PDF]