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240416s2024 xx |||||o 00| ||eng c |
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|a 10.1111/nph.19755
|2 doi
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|a pubmed24n1485.xml
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|a (DE-627)NLM371118956
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|a (NLM)38622771
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Li, Wen
|e verfasserin
|4 aut
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|a Litchi aspartic protease LcAP1 enhances plant resistance via suppressing cell death triggered by the pectate lyase PlPeL8 from Peronophythora litchii
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|c 2024
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 23.05.2024
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|a Date Revised 29.07.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2024 The Authors New Phytologist © 2024 New Phytologist Foundation.
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|a Plant cell death is regulated in plant-pathogen interactions. While some aspartic proteases (APs) participate in regulating programmed cell death or defense responses, the defense functions of most APs remain largely unknown. Here, we report on a virulence factor, PlPeL8, which is a pectate lyase found in the hemibiotrophic pathogen Peronophythora litchii. Through in vivo and in vitro assays, we confirmed the interaction between PlPeL8 and LcAP1 from litchi, and identified LcAP1 as a positive regulator of plant immunity. PlPeL8 induced cell death associated with NbSOBIR1 and NbMEK2. The 11 conserved residues of PlPeL8 were essential for inducing cell death and enhancing plant susceptibility. Twenty-three LcAPs suppressed cell death induced by PlPeL8 in Nicotiana benthamiana depending on their interaction with PlPeL8. The N-terminus of LcAP1 was required for inhibiting PlPeL8-triggered cell death and susceptibility. Furthermore, PlPeL8 led to higher susceptibility in NbAPs-silenced N. benthamiana than the GUS-control. Our results indicate the crucial roles of LcAP1 and its homologs in enhancing plant resistance via suppression of cell death triggered by PlPeL8, and LcAP1 represents a promising target for engineering disease resistance. Our study provides new insights into the role of plant cell death in the arms race between plants and hemibiotrophic pathogens
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|a Journal Article
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|a aspartic protease
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|a hemibiotroph
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|a oomycete
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|a pectate lyase
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|a plant cell death
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|a plant immunity
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|a Aspartic Acid Proteases
|2 NLM
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| 650 |
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|a EC 3.4.-
|2 NLM
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|a pectate lyase
|2 NLM
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| 650 |
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|a EC 4.2.2.2
|2 NLM
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| 650 |
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Polysaccharide-Lyases
|2 NLM
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| 650 |
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|a EC 4.2.2.-
|2 NLM
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| 700 |
1 |
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|a Li, Peng
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Deng, Yizhen
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhang, Zijing
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Situ, Junjian
|e verfasserin
|4 aut
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|a Huang, Ji
|e verfasserin
|4 aut
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|a Li, Minhui
|e verfasserin
|4 aut
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|a Xi, Pinggen
|e verfasserin
|4 aut
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|a Jiang, Zide
|e verfasserin
|4 aut
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| 700 |
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|a Kong, Guanghui
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t The New phytologist
|d 1979
|g 242(2024), 6 vom: 01. Juni, Seite 2682-2701
|w (DE-627)NLM09818248X
|x 1469-8137
|7 nnns
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| 773 |
1 |
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|g volume:242
|g year:2024
|g number:6
|g day:01
|g month:06
|g pages:2682-2701
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|u http://dx.doi.org/10.1111/nph.19755
|3 Volltext
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|d 242
|j 2024
|e 6
|b 01
|c 06
|h 2682-2701
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