Nature Immunology
- 7, 1243 - 1249 (2006)
Published online: 16 November 2006; | doi:10.1038/ni1410
Plant NBS-LRR proteins in pathogen sensing and host defenseBrody J DeYoung & Roger W Innes
Department of Biology, Indiana University, Bloomington, Indiana 47405, USA.
Correspondence should be addressed to Roger W Innes rinnes@indiana.edu 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 target proteins. However, some NBS-LRR proteins directly bind pathogen proteins. Association with either a modified host protein or a pathogen protein leads to conformational changes in the amino-terminal and LRR domains of plant NBS-LRR proteins. Such conformational alterations are thought to promote the exchange of ADP for ATP by the NBS domain, which activates 'downstream' signaling, by an unknown mechanism, leading to pathogen resistance.
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