NB-LRRs work a "bait and switch" on pathogens

Trends Plant Sci. 2009 Oct;14(10):521-9. doi: 10.1016/j.tplants.2009.08.001. Epub 2009 Aug 31.


Plant genomes encode large numbers of highly variable nucleotide binding leucine-rich repeat (NB-LRR) disease resistance proteins. These proteins have been studied extensively to understand their evolution and the molecular basis of their function. Multiple studies indicate that the C-terminal LRR domain plays a pivotal role in defining pathogen recognition specificity. However, a growing body of evidence suggests that the N-termini of NB-LRR proteins also function in pathogen recognition. To formulate a framework that can explain the underlying principles governing NB-LRR function while accommodating findings from different experimental systems, we present a "bait and switch" model. This model proposes a two-step recognition process involving interactions with both cellular cofactors (bait) and the LRR domain, which in turn activates the molecular switch leading to disease resistance.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Immunity, Innate / genetics
  • Immunity, Innate / physiology
  • Models, Biological
  • Plant Proteins / chemistry*
  • Plant Proteins / genetics
  • Plant Proteins / metabolism
  • Plant Proteins / physiology*
  • Protein Structure, Tertiary / genetics
  • Protein Structure, Tertiary / physiology
  • Proteins / chemistry*
  • Proteins / genetics
  • Proteins / metabolism
  • Proteins / physiology*


  • Plant Proteins
  • Proteins
  • leucine-rich repeat proteins