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(NAS Colloquium) Virulence and Defense in Host--Pathogen Interactions Common Features Between Plants and Animals (2001) / Chapter Skim
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A Framework for Interpreting the Leucine-rich Repeats of the Listeria Internalins
Pages 33-37

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From page 33...
... Roux, 75015 Paris, France The surface protein InlB of the bacterial pathogen Listeria monocytogenes is required for inducing phagocytosis in various nonphagocytic mammalian cell types in vitro. InlB causes tyrosine phosphorylation of host cell adaptor proteins, activation of phosphoinositide 3-kinase, and rearrangements of the actin cytoskeleton.
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From page 35...
... The calciums are not required for formation of protein structure and may instead act as metal ion bridges between InlB and mammalian cell surface receptors or binding proteins. The N-terminal cap and LRR regions of InlB are sufficient to elicit mammalian cell effects and to induce phagocytosis (38~.
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From page 36...
... Although the high sequence conservation of the internalin LRR allows strong predictions about protein-protein interaction sites based on the InlB structure, it does not lead as easily to predictions about target specificity. The challenge for the future will be in identifying binding partners for individual internalir~s and in determining how the LRR structural motif is used to generate a variety of specific functional interactions.
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From page 37...
... 32. Dixon, M
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Key Terms

  • internalin lrr
  • lrr proteins
  • inlb lrr
  • lrr region
  • host cell

  • lrr regions
  • charged residues
  • hydrogen bonds
  • mammalian cell
  • lrr motif

  • inducing phagocytosis
  • highly conserved
  • cell types
  • actin cytoskeleton
  • negatively charged

  • interaction surfaces
  • surface exposed
  • residues predicted
  • tyrosine phosphorylation
  • recently determined

  • lrr domain
  • mammalian cells
  • permissive cells
  • hydrophobic core
  • superhelical twist

  • positively charged
  • proteins inla
  • cell surface
  • plant immune
  • cell signaling


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