Perception of the chitin oligosaccharides contributes to disease resistance to blast fungus Magnaporthe oryzae in rice

Chitin is a component of fungal cell walls, and its fragments act as elicitors in many plants. The plasma membrane glycoprotein CEBiP, which possesses LysM domains, is a receptor for the chitin elicitor (CE) in rice. Here, we report that the perception of CE by CEBiP contributes to disease resistanc...

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Veröffentlicht in:The Plant journal : for cell and molecular biology 2010-10, Vol.64 (2), p.343-354
Hauptverfasser: Kishimoto, Kyutaro, Kouzai, Yusuke, Kaku, Hanae, Shibuya, Naoto, Minami, Eiichi, Nishizawa, Yoko
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container_title The Plant journal : for cell and molecular biology
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creator Kishimoto, Kyutaro
Kouzai, Yusuke
Kaku, Hanae
Shibuya, Naoto
Minami, Eiichi
Nishizawa, Yoko
description Chitin is a component of fungal cell walls, and its fragments act as elicitors in many plants. The plasma membrane glycoprotein CEBiP, which possesses LysM domains, is a receptor for the chitin elicitor (CE) in rice. Here, we report that the perception of CE by CEBiP contributes to disease resistance against the rice blast fungus, Magnaporthe oryzae, and that enhanced responses to CE by engineering CEBiP increase disease tolerance. Knockdown of CEBiP expression allowed increased spread of the infection hyphae. To enhance defense responses to CE, we constructed chimeric genes composed of CEBiP and Xa21, which mediate resistance to rice bacterial leaf blight. The expression of either CRXa1 or CRXa3, each of which contains the whole extracellular portion of CEBiP, the whole intracellular domain of XA21, and the transmembrane domain from either CEBiP or XA21, induced cell death accompanied by an increased production of reactive oxygen and nitrogen species after treatment with CE. Rice plants expressing the chimeric receptor exhibited necrotic lesions in response to CE and became more resistant to M. oryzae. Deletion of the first LysM domain in CRXA1 abolished these cellular responses. These results suggest that CEs are produced and recognized through the LysM domain of CEBiP during the interaction between rice and M. oryzae and imply that engineering pattern recognition receptors represents a new strategy for crop protection against fungal diseases.
doi_str_mv 10.1111/j.1365-313x.2010.04328.x
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The plasma membrane glycoprotein CEBiP, which possesses LysM domains, is a receptor for the chitin elicitor (CE) in rice. Here, we report that the perception of CE by CEBiP contributes to disease resistance against the rice blast fungus, Magnaporthe oryzae, and that enhanced responses to CE by engineering CEBiP increase disease tolerance. Knockdown of CEBiP expression allowed increased spread of the infection hyphae. To enhance defense responses to CE, we constructed chimeric genes composed of CEBiP and Xa21, which mediate resistance to rice bacterial leaf blight. The expression of either CRXa1 or CRXa3, each of which contains the whole extracellular portion of CEBiP, the whole intracellular domain of XA21, and the transmembrane domain from either CEBiP or XA21, induced cell death accompanied by an increased production of reactive oxygen and nitrogen species after treatment with CE. 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The plasma membrane glycoprotein CEBiP, which possesses LysM domains, is a receptor for the chitin elicitor (CE) in rice. Here, we report that the perception of CE by CEBiP contributes to disease resistance against the rice blast fungus, Magnaporthe oryzae, and that enhanced responses to CE by engineering CEBiP increase disease tolerance. Knockdown of CEBiP expression allowed increased spread of the infection hyphae. To enhance defense responses to CE, we constructed chimeric genes composed of CEBiP and Xa21, which mediate resistance to rice bacterial leaf blight. The expression of either CRXa1 or CRXa3, each of which contains the whole extracellular portion of CEBiP, the whole intracellular domain of XA21, and the transmembrane domain from either CEBiP or XA21, induced cell death accompanied by an increased production of reactive oxygen and nitrogen species after treatment with CE. 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Rice plants expressing the chimeric receptor exhibited necrotic lesions in response to CE and became more resistant to M. oryzae. Deletion of the first LysM domain in CRXA1 abolished these cellular responses. These results suggest that CEs are produced and recognized through the LysM domain of CEBiP during the interaction between rice and M. oryzae and imply that engineering pattern recognition receptors represents a new strategy for crop protection against fungal diseases.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>21070413</pmid><doi>10.1111/j.1365-313x.2010.04328.x</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record>
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subjects Ageing, cell death
Biological and medical sciences
Carbohydrates
Cell Death
Cell physiology
Cell receptors
Cell structures and functions
Cell walls
Cellular biology
chimeric receptor
Chitin
Chitin - metabolism
chitin signal
Crop protection
Disease resistance
Disease tolerance
Fertility
Fundamental and applied biological sciences. Psychology
Fungi
Gene expression
Glycoproteins
Host-Pathogen Interactions
HR cell death
Hyphae
Infection
Leaf blight
Magnaporthe - physiology
Magnaporthe grisea
MAMP-triggered immunity
Miscellaneous
Molecular and cellular biology
Nitrogen
oligosaccharides
Oligosaccharides - metabolism
Oryza - immunology
Oryza - metabolism
Oryza - microbiology
Oryza sativa
Oxygen
Pattern recognition
Perception
Plant biology
Plant Diseases
Plant physiology and development
Plant Proteins - genetics
Plant resistance
Plants, Genetically Modified - immunology
Plants, Genetically Modified - metabolism
Plants, Genetically Modified - microbiology
Plasma membranes
Protein-Serine-Threonine Kinases - genetics
Recombinant Fusion Proteins - metabolism
rice blast
rice blast fungus
Transmembrane domains
title Perception of the chitin oligosaccharides contributes to disease resistance to blast fungus Magnaporthe oryzae in rice
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