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J. Biol. Chem., Vol. 282, Issue 9, 6803-6811, March 2, 2007

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Chemical Interference of Pathogen-associated Molecular Pattern-triggered Immune Responses in Arabidopsis Reveals a Potential Role for Fatty-acid Synthase Type II Complex-derived Lipid Signals^*

Mario Serrano, Silke Robatzek, Martha Torres, Erich Kombrink, Imre E. Somssich, Mike Robinson, and Paul Schulze-Lefert¹

From the Department of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linné Weg 10, 50829 Cologne, Germany and Syngenta Jealott's Hill International Research Centre, Bracknell, Berkshire RG42 6EY, United Kingdom

We describe an experimental setup using submerged cultures of Arabidopsis seedlings in 96-well microtiter plates that permits chemical intervention of rapid elicitor-mediated immune responses. Screening of a chemical library comprising 120 small molecules with known biological activities revealed four compounds reducing cellulysin- or flg22-activated gene expression of the early pathogen-associated molecular patterns (PAMP)-responsive ATL2 gene. One chemical, oxytriazine, was found to induce ATL2 gene expression in the absence of PAMP. By monitoring additional flg22-triggered immediate early plant responses, we present evidence that two compounds, triclosan and fluazinam, interfere with the accumulation of reactive oxygen species and internalization of the activated plasma membrane resident FLS2 immune receptor. Using triclosan structure types and enzyme activity inhibition assays, Arabidopsis MOD1 enoyl-acyl carrier protein reductase, a subunit of the fatty-acid synthase type II (FAS II) complex, was identified as a likely cellular target of triclosan. Inhibition of all tested elicitor-triggered early immune responses by triclosan indicates a potential role for signaling lipids in flg22-triggered immunity. Chemical profiling of eca mutants, each showing deregulated ATL2 gene expression, with the identified compounds revealed mutantspecific response patterns and allowed us to deduce tentative action sites of ECA genes relative to the compound targets.

Received for publication, September 12, 2006 , and in revised form, December 12, 2006.

^* This work was supported by a Max Planck post-doctoral fellowship (to M. S.) and in part by Fonds der Chemischen Industrie, Germany. 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1-4 and Table 1.

¹ To whom correspondence should be addressed. Tel.: 49-221-5062-350; Fax: 49-221-5062-353; E-mail: schlef{at}mpiz-koeln.mpg.de.

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