HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 279, Issue 2, 1132-1140, January 9, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/2/1132    most recent M308552200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Fliegmann, J. Articles by Ebel, J. Search for Related Content PubMed PubMed Citation Articles by Fliegmann, J. Articles by Ebel, J. Social Bookmarking                      What's this?

An Ancient Enzyme Domain Hidden in the Putative -Glucan Elicitor Receptor of Soybean May Play an Active Part in the Perception of Pathogen-associated Molecular Patterns during Broad Host Resistance^*

Judith Fliegmann, Axel Mithöfer¶, Gerhard Wanner, and Jürgen Ebel

From the Department Biologie I/Botanik, Ludwig-Maximilians Universität, Menzinger Str. 67, D-80638 München, and the ^¶MPI für Chemische Ökologie, Beutenberg Campus, Hans-Knöll-Str. 8, D-07745 Jena, Germany

A successful defense against potential pathogens requires that a host organism is able to discriminate between self and nonself structures. Soybean (Glycine max L.) exploits a specific molecular pattern, a 1,6--linked and 1,3--branched heptaglucoside (HG), present in cell walls of the oomycetal pathogen Phytophthora sojae, as a signal compound eliciting the onset of defense reactions. The specific and high affinity HG-binding site is contained in the -glucan-binding protein (GBP), which in turn is part of a proposed receptor complex. The ability to perceive and respond to Phytophthora cell wall-derived -glucan elicitors is exclusive to plants that belong to the Fabaceae. However, we propose that the presence of the GBP is essential, but not sufficient for -glucan elicitor-dependent disease resistance because genes encoding GBP-related proteins can be retrieved from many plant species. Furthermore, we show that the GBP is composed of two different carbohydrateactive protein domains, one containing the -glucan-binding site, and the other related to glucan endoglucosidases of fungal origin. The glucan hydrolase displays most likely an endo-specific mode of action, cleaving only 1,3--D-glucosidic linkages of oligoglucosides consisting of at least four moieties. Thus, the intrinsic endo-1,3--glucanase activity of the GBP is perfectly suited during initial contact with Phytophthora to release oligoglucoside fragments enriched in motifs that constitute ligands for the high affinity binding site present in the same protein. The concept of innate immunity in plants receives substantial support by this highly sophisticated system using ancient enzyme modules as an active part of the recognition mechanism.

Received for publication, August 4, 2003 , and in revised form, October 2, 2003.

^* This work was supported in part by European Community Human Potential Programme Contract HPRN-CT-2002-00251, SACC-SIG-NET, and Deutsche Forschungsgemeinschaft Grant SFB369. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 49-89-17861202; Fax: 49-89-1782274; E-mail: judith.fliegmann{at}lmu.de.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. Bernoux, T. Timmers, A. Jauneau, C. Briere, P. J.G.M. de Wit, Y. Marco, and L. Deslandes RD19, an Arabidopsis Cysteine Protease Required for RRS1-R-Mediated Resistance, Is Relocalized to the Nucleus by the Ralstonia solanacearum PopP2 Effector PLANT CELL, August 1, 2008; 20(8): 2252 - 2264. [Abstract] [Full Text] [PDF]

				N. Geldner and S. Robatzek Plant Receptors Go Endosomal: A Moving View on Signal Transduction Plant Physiology, August 1, 2008; 147(4): 1565 - 1574. [Full Text] [PDF]

				A. Mithofer and W. Boland Recognition of Herbivory-Associated Molecular Patterns Plant Physiology, March 1, 2008; 146(3): 825 - 831. [Full Text] [PDF]

				K. A.E. van't Slot, A. Gierlich, and W. Knogge A Single Binding Site Mediates Resistance- and Disease-Associated Activities of the Effector Protein NIP1 from the Barley Pathogen Rhynchosporium secalis Plant Physiology, July 1, 2007; 144(3): 1654 - 1666. [Abstract] [Full Text] [PDF]

				A. L. van Bueren, C. Morland, H. J. Gilbert, and A. B. Boraston Family 6 Carbohydrate Binding Modules Recognize the Non-reducing End of {beta}-1,3-Linked Glucans by Presenting a Unique Ligand Binding Surface J. Biol. Chem., January 7, 2005; 280(1): 530 - 537. [Abstract] [Full Text] [PDF]

				Y. Adachi, T. Ishii, Y. Ikeda, A. Hoshino, H. Tamura, J. Aketagawa, S. Tanaka, and N. Ohno Characterization of {beta}-Glucan Recognition Site on C-Type Lectin, Dectin 1 Infect. Immun., July 1, 2004; 72(7): 4159 - 4171. [Abstract] [Full Text] [PDF]