The Intracellular Immune Receptor Sw-5b Confers Broad-Spectrum Resistance to Tospoviruses through Recognition of a Conserved 21-Amino Acid Viral Effector Epitope. Issue 9 (16th August 2017)
- Record Type:
- Journal Article
- Title:
- The Intracellular Immune Receptor Sw-5b Confers Broad-Spectrum Resistance to Tospoviruses through Recognition of a Conserved 21-Amino Acid Viral Effector Epitope. Issue 9 (16th August 2017)
- Main Title:
- The Intracellular Immune Receptor Sw-5b Confers Broad-Spectrum Resistance to Tospoviruses through Recognition of a Conserved 21-Amino Acid Viral Effector Epitope
- Authors:
- Zhu, Min
Jiang, Lei
Bai, Baohui
Zhao, Wenyang
Chen, Xiaojiao
Li, Jia
Liu, Yong
Chen, Zhengqiang
Wang, Boting
Wang, Chunli
Wu, Qian
Shen, Qianhua
Dinesh-Kumar, Savithramma P.
Tao, Xiaorong - Abstract:
- Abstract : A plant intracellular immune receptor mediates broad-spectrum resistance by recognizing a small conserved PAMP-like region within the pathogen protein. Abstract: Plants use both cell surface-resident pattern recognition receptors (PRRs) and intracellular nucleotide binding leucine-rich repeat (NLR) receptors to detect various pathogens. Plant PRRs typically recognize conserved pathogen-associated molecular patterns (PAMPs) to provide broad-spectrum resistance. By contrast, plant NLRs generally detect pathogen strain-specific effectors and confer race-specific resistance. Here, we demonstrate that the tomato ( Solanum lycopersicum ) NLR Sw-5b confers broad-spectrum resistance against American-type tospoviruses by recognizing a conserved 21-amino acid peptide region within viral movement protein NSm (NSm 21 ). Sw-5b NB-ARC-LRR domains directly associate with NSm 21 in vitro and in planta. Domain swap, site-directed mutagenesis and structure modeling analyses identified four polymorphic sites in the Sw-5b LRR domain that are critical for the recognition of NSm 21 . Furthermore, recognition of NSm 21 by Sw-5b likely disturbs the residues adjacent to R927 in the LRR domain to weaken the intramolecular interaction between LRR and NB-ARC domains, thus translating recognition of NSm 21 into activation of Sw-5b. Natural variation analysis of Sw-5b homologs from wild tomato species of South America revealed that the four polymorphic sites in the Sw-5b LRR domain wereAbstract : A plant intracellular immune receptor mediates broad-spectrum resistance by recognizing a small conserved PAMP-like region within the pathogen protein. Abstract: Plants use both cell surface-resident pattern recognition receptors (PRRs) and intracellular nucleotide binding leucine-rich repeat (NLR) receptors to detect various pathogens. Plant PRRs typically recognize conserved pathogen-associated molecular patterns (PAMPs) to provide broad-spectrum resistance. By contrast, plant NLRs generally detect pathogen strain-specific effectors and confer race-specific resistance. Here, we demonstrate that the tomato ( Solanum lycopersicum ) NLR Sw-5b confers broad-spectrum resistance against American-type tospoviruses by recognizing a conserved 21-amino acid peptide region within viral movement protein NSm (NSm 21 ). Sw-5b NB-ARC-LRR domains directly associate with NSm 21 in vitro and in planta. Domain swap, site-directed mutagenesis and structure modeling analyses identified four polymorphic sites in the Sw-5b LRR domain that are critical for the recognition of NSm 21 . Furthermore, recognition of NSm 21 by Sw-5b likely disturbs the residues adjacent to R927 in the LRR domain to weaken the intramolecular interaction between LRR and NB-ARC domains, thus translating recognition of NSm 21 into activation of Sw-5b. Natural variation analysis of Sw-5b homologs from wild tomato species of South America revealed that the four polymorphic sites in the Sw-5b LRR domain were positively selected during evolution and are all necessary to confer resistance to tospovirus. The results described here provide a new example of a plant NLR mediating broad-spectrum resistance through recognition of a small conserved PAMP -like region within the pathogen effector. … (more)
- Is Part Of:
- The Plant Cell. Volume 29:Issue 9(2017)
- Journal:
- The Plant Cell
- Issue:
- Volume 29:Issue 9(2017)
- Issue Display:
- Volume 29, Issue 9 (2017)
- Year:
- 2017
- Volume:
- 29
- Issue:
- 9
- Issue Sort Value:
- 2017-0029-0009-0000
- Page Start:
- 2214
- Page End:
- 2232
- Publication Date:
- 2017-08-16
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.17.00180 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16315.xml