High affinity recognition of a Phytophthora protein by Arabidopsis via an RGD motif

V. Senchou, R.L. Weide, A. Carrasco, H. Bouyssou, R. Pont-Lezica, F. Govers, H. Canut

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The RGD tripeptide sequence, a cell adhesion motif present in several extracellular matrix proteins of mammalians, is involved in numerous plant processes. In plant-pathogen interactions, the RGD motif is believed to reduce plant defence responses by disrupting adhesions between the cell wall and plasma membrane. Photoaffinity cross-linking of [I-125]-azido-RGD heptapeptide in the presence of purified plasma membrane vesicles of Arabidopsis thaliana led to label incorporation into a single protein with an apparent molecular mass of 80 kDa. Incorporation could be prevented by excess RGD peptides, but also by the IPI-O protein, an RGD-containing protein secreted by the oomycete plant pathogen Phytophthora infestans. Hydrophobic cluster analysis revealed that the RGD motif of IPI-O (positions 53-56) is readily accessible for interactions. Single amino acid mutations in the RGD motif in IPI-O (of Asp(56) into Glu or Ala) resulted in the loss of protection of the 80-kDa protein from labelling. Thus, the interaction between the two proteins is mediated through RGD recognition and the 80-kDa RGD-binding protein has the characteristics of a receptor for IPI-O. The IPI-O protein also disrupted cell wall-plasma membrane adhesions in plasmolysed A. thaliana cells, whereas IPI-O proteins mutated in the RGD motif (D56A and D56E) did not.
Original languageEnglish
Pages (from-to)502-509
JournalCellular and Molecular Life Sciences
Issue number4
Publication statusPublished - 2004


  • plant defense responses
  • plasma-membrane
  • cell-wall
  • extracellular-matrix
  • ipio gene
  • thaliana
  • integrins
  • sequence
  • receptors
  • infestans


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