Dokument

Zusammenfassung:
Der Brandpilz Ustilago maydis benötigt während der Interaktion mit seiner Wirtspflanze Mais eine Vielzahl sekretierter Effektoren zur Etablierung der Biotropie. Eine Deletion des Gens um01987, das für den sekretierten Effektor Pep1 (protein essential during penetration 1) codiert, führt zum vollständigen Verlust der Pathogenität. Auf Penetrationsversuche der pep1-Deletionsmutante reagiert die Maispflanze mit der Induktion verschiedener Abwehrmechanismen wie der Bildung von Papillen, der Anreicherung reaktiver Sauerstoffspezies und nekrotischen Läsionen. Pep1 lokalisiert in der biotrophen Interaktionszone und ist in verschiedenen Brandpilzarten konserviert. In der vorliegenden Arbeit wurde die Funktion von Pep1 durch biochemische und molekularbiologische Methoden charakterisiert. So konnte gezeigt werden, dass heterolog in Escherichia coli exprimiertes Pep1 den oxidative burst in Mais inhibieren kann. Eine Behandlung von Maispflanzen mit dem Radikalfänger Ascorbat hatte verminderte Abwehrreaktionen gegenüber Infektionen mit der pep1-Deletionsmutante zur Folge. Weiterhin wurde gezeigt, dass Pep1 die Aktivität einer Klasse-III-Peroxidase aus Meerrettich in vitro hemmt. Klasse-III-Peroxidasen spielen eine zentrale Rolle in der Produktion reaktiver Sauerstoffspezies beim oxidative burst. Bei Infektionen von Mais mit der pep1-Deletionsmutante ist die sekretierte Peroxidase-12 (POX12) transkriptionell induziert. Durch Bimolekulare Fluoreszenzkompementatiion und Hefe-2-Hybrid-Experimente konnte eine direkte Interaktion von Pep1 mit POX12 nachgewiesen werden. Durch virusinduziertes Gen-Silencing von pox12 in Mais konnte eine partielle Rettung des Δpep1-Phänotyps erreicht werden. Das Silencing von pox12 bewirkte verminderte Abwehrreaktionen der Wirtspflanze wie z. B. Papillenbildungen an Penetrationsstellen, so dass die Hyphen der pep1-Deletionsmutante in der Folge die Epidermiszellen penetrieren konnten. Darüber hinaus konnten Orthologe von pep1 in weiteren Brandpilzspezies identifiziert werden. Es wurde in vitro gezeigt, dass die Pep1-Orthologe aus Ustilago avenae, Ustilago nuda und Melanopsichium pennsylvanicum ebenfalls als Peroxidaseinhibitoren agieren. Weiterhin wurde die Inhibition apoplastischer Peroxidasen aus verschiedenen Wirtspflanzen durch Pep1 nachgewiesen. Schließlich wurde die Funktion der identifizierten Pep1-Orthologe in Infektionen von Mais mit U. maydis bestätigt. Diese Ergebnisse sprechen für eine Rolle von Pep1 als Inhibitor von Peroxidasen, einer zentralen Komponente der basalen pflanzlichen Abwehrreaktion.

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