Publikationsserver der Universitätsbibliothek Marburg
Titel:Appressorienbildung von Ustilago maydis auf hydrophoben Oberflächen: Regulation durch Membranproteine
Autor:Lanver, Daniel
Weitere Beteiligte: Kahmann, Regine (Prof. Dr.)
Veröffentlicht:2011
URI:https://archiv.ub.uni-marburg.de/diss/z2011/0126
URN: urn:nbn:de:hebis:04-z2011-01269
DOI: https://doi.org/10.17192/z2011.0126
DDC: Biowissenschaften, Biologie
Titel (trans.):Appressorium formation of Ustilago maydis on hydrophobic surfaces: Regulation through membrane proteins
Publikationsdatum:2011-08-10
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
Phytopathogene Pilze, Mucin, MAP-Kinase, Appressorium, map-kinase, appressorium, phytopathogenic fungi, mucin, Rezeptor, receptor, virulence, Virulenz

Zusammenfassung:
Ustilago maydis ist der Erreger des Maisbeulenbrandes. Die pathogene Entwicklung wird durch Fusion kompatibler Zellen und der Bildung eines dikaryotischen Filaments initiiert. Auf der Pflanzenoberfläche bildet U. maydis Appressorien aus, die das Eindringen des Pilzes in die Pflanze ermöglichen. Die Appressorienbildung wird durch die Hydrophobizität der Blattoberfläche und Cutin Monomere stimuliert. Die pathogene Entwicklung von U. maydis wird durch eine konservierte, zum FG (filamentous growth)-Signalweg in Saccharomyces cerevisiae homologe, MAP-Kinase Kaskade gesteuert. In Hefe agieren zwei Plasmamembranproteine, Sho1p und Msb2p, an der Spitze des MAP-Kinase Signalwegs. In dieser Arbeit wurden Sho1- und Msb2-verwandte Proteine in U. maydis untersucht. Es konnte gezeigt werden, dass Sho1 und Msb2 essentiell für die Virulenz von U. maydis sind. Genetische Analysen ergaben, dass Sho1 und Msb2 oberhalb der pathogenitätsrelevanten MAP-Kinase Kaskade agieren. Für Sho1 wurde zudem gezeigt, dass es die MAP-Kinase Kpp6 destabilisiert, indem es direkt mit der N-terminalen Domäne von Kpp6 interagiert. Dies dient wahrscheinlich der Feinregulation der Kpp6 Aktivität. Es konnte nachgewiesen werden, dass Sho1 und Msb2 spezifisch die Appressorienbildung regulieren, aber für die Zellfusion sowie filamentöses Wachstum nicht benötigt werden. Ferner waren sho1 und msb2 Mutanten während der morphologischen Differenzierung auf hydrophoben Oberflächen eingeschränkt, während die Reaktion auf Cutin Monomere nicht beeinträchtigt war. Dies deutet darauf hin, dass Sho1 und Msb2, die beide in der Plasmamembran lokalisieren, bei der Perzeption von Oberflächen beteiligt sind. Msb2, welches zur Familie der Transmembranmucine gehört, wird in ein zelluläres und ein extrazelluläres Fragment prozessiert. Beide Proteindomänen werden für die Funktion von Msb2 benötigt. Da die hoch glycosylierte extrazelluläre Domäne an die Umgebung abgegeben wird, werden zusätzliche Funktionen von Msb2 in der extrazellulären Matrix vermutet, wie z.B. die Vermittlung der Adhäsion zwischen Filamenten und Oberflächen. Transkriptomanalysen unter Appressorien-induzierenden in vitro Bedingungen zeigten, dass Sho1 und Msb2 notwendig für die Expression von potentiell sekretierten Zellwand-degradierenden Enzymen sind. Ferner wurden sekretierte Effektoren, die essentiell für die biotrophe Interaktion von U. maydis mit seiner Wirtspflanze sind, in Abhängigkeit von Sho1 und Msb2 exprimiert. Dies zeigt, dass U. maydis durch Sho1 und Msb2 auf die biotrophe Entwicklung vorbereitet wird, noch während die Hyphen auf der Pflanzenoberfläche wachsen. Da Sho1 und Msb2 in phytopathogenen Pilzen konservierte Proteine sind, könnten sie generelle Virulenzfaktoren darstellen.

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