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JXB Advance Access originally published online on March 23, 2006
Journal of Experimental Botany 2006 57(6):1461-1469; doi:10.1093/jxb/erj127
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© The Author [2006]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

RESEARCH PAPER

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

Alejandro Pérez-de-Luque1,*, Clara I. González-Verdejo2, M. Dolores Lozano1, Miguel A. Dita1, José I. Cubero3, Pablo González-Melendi4, María C. Risueño4 and Diego Rubiales1

1CSIC, Instituto de Agricultura Sostenible, E-14080 Córdoba, Apdo. 4084, Spain
2IFAPA-CICE (Junta de Andalucia), CIFA ‘Alameda del Obispo’, Área de Mejora y Biotecnología, E-14080 Cordoba, Apdo. 3092, Spain
3ETSIAM-UCO, Departamento de Genética, E-14080 Córdoba, Apdo. 3048, Spain
4CSIC, Centro de Investigaciones Biológicas, Departamento de Plant Development and Nuclear Organization, Ramiro de Maeztu 9, E-28040 Madrid, Spain

* To whom correspondence should be addressed. E-mail: bb2pelua{at}uco.es

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 ß-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.

Key words: Confocal microscopy, cytochemistry, glucanase, in situ hybridization, Orobanche crenata, parasitic plants, peroxidase, Pisum sativum, protein cross-linking, resistance


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This article has been cited by other articles:


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M. D. Lozano-Baena, E. Prats, M. T. Moreno, D. Rubiales, and A. Perez-de-Luque
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S. Echevarria-Zomeno, A. Perez-de-Luque, J. Jorrin, and A. M. Maldonado
Pre-haustorial resistance to broomrape (Orobanche cumana) in sunflower (Helianthus annuus): cytochemical studies
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[Abstract] [Full Text] [PDF]


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