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Glycobiology Advance Access published online on April 1, 2008
Glycobiology, doi:10.1093/glycob/cwn027
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© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Egg box conformation of oligogalacturonides. The time-dependent stabilization of the elicitor-active conformation increases its biological activity

Juan Carlos Cabrera, Aurelien Boland, Johan Messiaen, Pierre Cambier and Pierre Van Cutsem

Unité de Recherche en Biologie Cellulaire Végétale, Facultés Universitaires Notre-Dame de la Paix, Namur B-5000, Belgium

Corresponding author: Pierre Van Cutsem, Unité de Recherche en Biologie Cellulaire Végétale, Facultés Universitaires Notre-Dame de la Paix, Rue de Bruxelles 61, Namur, B-5000, Belgium; Telephone number: +32 (0) 8172 4414, E-mail address: pierre.vancutsem{at}fundp.ac.be

Received on February 26, 2008; accepted on March 24, 2008

Circular dichroism spectrometry was used on oligogalacturonides (OGA) and showed the existence of a calcium/sodium induced conformational state that is intermediate between single isolated chains and calcium-associated multimer chains. This conformation is interpreted as being egg box dimers. Using the 2F4 monoclonal antibody that specifically binds such an egg box dimer conformation of pectin, the stability of OGA dimers was investigated over a period of several days. The extent to which egg box dimers were recognized by the antibody was dependent on temperature and duration of pre-incubation of the OGA. This suggests a "maturation" process of the egg-box structure that consists in a progressive increase in length of the junction sequences between two chains that slide along each other in order to form a maximum number of calcium bridges and dimer ends. The maturation of egg boxes induced both a significant increase in their binding to Wall Associated Kinase 1 (WAK1) and an increased extracellular alkalinization when applied to Arabidopsis thaliana cell suspensions. Chemical modification of the reducing end of the oligogalacturonides largely diminished their elicitating activity but did not hinder neither dimerization nor binding of these end-reduced egg boxes to WAK1. We conclude that there are at least two different perception systems for egg box dimers. One binds egg box junctions and the other one binds egg box ends. The relevance of these results is discussed in terms of pectic signal perception and plant-pathogen interaction.

Key words: Oligogalacturonides / Egg box / Elicitation / Arabidopsis / Pectin


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