2006
DOI: 10.1038/ni1410
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Plant NBS-LRR proteins in pathogen sensing and host defense

Abstract: Plant proteins belonging to the nucleotide-binding site-leucine-rich repeat (NBS-LRR) family are used for pathogen detection. Like the mammalian Nod-LRR protein 'sensors' that detect intracellular conserved pathogen-associated molecular patterns, plant NBS-LRR proteins detect pathogen-associated proteins, most often the effector molecules of pathogens responsible for virulence. Many virulence proteins are detected indirectly by plant NBS-LRR proteins from modifications the virulence proteins inflict on host ta… Show more

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Cited by 635 publications
(480 citation statements)
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“…Rather than directly engaging a pathogen-derived product, NLRX1 seems to function as a modulator of PAMP receptors (MOPR) by affecting the interaction of the pathogen receptor RIG-I (and possibly MDA-5) with MAVS. This mechanism is more in-line with the Guard hypothesis proposed for the indirect detection of pathogen products by plant R proteins 21,22 . Because both NLRX1 and RIG-I interact with the CARD domain of MAVS, a probable scenario is that NLRX1 and RIG-I compete for binding with the CARD domain of MAVS, with opposing outcomes.…”
supporting
confidence: 85%
“…Rather than directly engaging a pathogen-derived product, NLRX1 seems to function as a modulator of PAMP receptors (MOPR) by affecting the interaction of the pathogen receptor RIG-I (and possibly MDA-5) with MAVS. This mechanism is more in-line with the Guard hypothesis proposed for the indirect detection of pathogen products by plant R proteins 21,22 . Because both NLRX1 and RIG-I interact with the CARD domain of MAVS, a probable scenario is that NLRX1 and RIG-I compete for binding with the CARD domain of MAVS, with opposing outcomes.…”
supporting
confidence: 85%
“…While some motifs have been found in these variable regions, the major feature ascribed to these proteins, a coiled-coil domain, has never been demonstrated, only computationally predicted. Since oligomerization of NB-LRRassociated coiled-coil domains has not been reported, and cellular proteins that interact with this domain show no common structures, it would seem that the existence of a coiled-coil structure either has a role in protein conformation or is simply an artifact of the prediction programs (Deyoung and Innes 2006).…”
Section: Discussionmentioning
confidence: 99%
“…LRR domains are present in proteins with diverse functions, providing a framework for the formation of protein-protein interactions. In plants, they have been implicated in innate immunity signaling pathways (DeYoung and Innes, 2006). Several aphid resistance genes, conferring phloem-specific resistance, such as the mi gene in tomato (Solanum lycopersicum) and the vat gene in C. melo, encode nucleotide-binding site-LRR proteins (Kaloshian et al, 2000;Dogimont et al, 2008), suggesting a potential role, in sieve elements, in interactions with phloem-feeding insects.…”
Section: Survey Of Phloem Sap Proteinsmentioning
confidence: 99%