Protein cross-linking, peroxidase and beta-1,3-endoglucanase involved in resistance of pea against Orobanche crenata

J Exp Bot. 2006;57(6):1461-9. doi: 10.1093/jxb/erj127. Epub 2006 Mar 23.

Abstract

Root holoparasitic angiosperms, like Orobanche spp, completely lack chlorophyll and totally depend on their host for their supply of nutrients. O. crenata is a severe constraint to the cultivation of legumes and breeding for resistance remains the most economical, feasible, and environmentally friendly method of control. Due to the lack of resistance in commercial pea cultivars, the use of wild relatives for breeding is necessary, and an understanding of the mechanisms underlying host resistance is needed in order to improve screening for resistance in breeding programmes. Compatible and incompatible interactions between O. crenata and pea have been studied using cytochemical procedures. The parasite was stopped in the host cortex before reaching the central cylinder, and accumulation of H2O2, peroxidases, and callose were detected in neighbouring cells. Protein cross-linking in the host cell walls appears as the mechanism of defence, halting penetration of the parasite. In situ hybridization studies have also shown that a peroxidase and a beta-glucanase are differently expressed in cells of the resistant host (Pf651) near the penetration point. The role of these proteins in the resistance to O. crenata is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cellulases / genetics
  • Cellulases / metabolism*
  • Fluorescent Antibody Technique
  • Glucan Endo-1,3-beta-D-Glucosidase / genetics
  • Glucan Endo-1,3-beta-D-Glucosidase / metabolism*
  • In Situ Hybridization
  • Microscopy, Confocal
  • Orobanche / physiology*
  • Peroxidase / genetics
  • Peroxidase / metabolism*
  • Pisum sativum / immunology
  • Pisum sativum / microbiology*
  • Pisum sativum / physiology
  • Plant Roots / immunology*
  • Plant Roots / microbiology
  • Plant Roots / physiology

Substances

  • Peroxidase
  • Cellulases
  • Glucan Endo-1,3-beta-D-Glucosidase