Publikationsserver der Universitätsbibliothek Marburg
Titel:Vergleichende Struktur-/Funktionsanalyse von Adhäsionsdomänen pathogener und nicht-pathogener Hefen
Autor:Kock, Michael Alexander
Weitere Beteiligte: Essen, Lars-Oliver (Prof. Dr.)
Veröffentlicht:2015
URI:https://archiv.ub.uni-marburg.de/diss/z2015/0343
URN: urn:nbn:de:hebis:04-z2015-03434
DOI: https://doi.org/10.17192/z2015.0343
DDC: Chemie
Titel (trans.):Comparative structure/function analysis of adhesion domains of pathogenic and non-pathogenic yeasts
Publikationsdatum:2016-01-25
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
Pichia pastoris, Saccharomyces cerevisiae, Biochemie, Torulopsis glabrata, protein crystallography, biochemistry, adhesin, Adhäsine, Proteinkristallographie, yeast

Zusammenfassung:
Hefen sind in der Lage sich an unterschiedlichste Umweltbedingungen anzupassen und dadurch eine große Anzahl von Habitaten zu besiedeln. Die erste Kontaktfläche mit ihrer Umwelt bilden Hefen mit ihrer einzigartigen Zellwand und den darin integrierten Zellwandproteinen. Ein großer Teil dieser Proteine, darunter die GPI-verankerten Zellwandproteine (GPI-CWP), dient zur Zell/Zell- oder Zell/Substrat-Adhäsion und spielt damit eine essentielle Rolle in der Lebensweise der Hefen. Einige dieser Proteine sind in der Lage Glycanstrukturen zu binden und zeigen einen gemeinsamen Domänenaufbau. Einer C-Typ-Lektin-artigen A-Domäne folgt eine mittlere, hoch repetitive und O-glycosylierte B-Region. Die Fixierung dieser Zellwandproteine gelingt durch die Transglycosylierung eines in der C-Domäne befindlichen Glycosylphosphatidylinositolankers. Die Glycanbindedomäne basiert strukturell auf der PA14-Domäne des protektiven Antigens von Bacillus anthracis. Sie enthält ein ungewöhnliches Motiv aus zwei konsekutiven, mit einer cis-Peptidbindung verbundenen Aspartaten, welche ein Ca2+-Ion komplexieren. Zusammen mit Aminosäureresten aus verschiedenen Schleifenbereichen wird hiermit die Affinität und Spezifität der Glycanbindung erzeugt. In dieser Arbeit gelang es, mittels einer sorgfältigen bioinformatischen und phylogenetischen Studie, neue Subtypen mit konservierten Eigenschaften dieser Adhäsinfamilie in Ascomyceten zu identifizieren. Cea1A, ein charakteristisches Mitglied des Pichia-Subtyps, konnte hierbei funktionell sowie strukturell charakterisiert werden. Dieses Adhäsin bindet an N-Acetylglucosamin und vermittelt damit die spezifische und hochaffine Erkennung nicht-reduzierender Enden nicht-kristalliner chitinöser Polymere. Die Struktur von Cea1A zeigt, neben einer neuartigen, stielförmigen Subdomäne, einen eigenständigen Bindungsmodus, welcher eine kompakte Bindungstasche und ladungsgetriebene Interaktionen verbindet. Cea1A könnte hiermit die molekulare Grundlage der Vergesellschaftung von Hefen mit Insekten darstellen. PpFlo1A, ein weiteres Adhäsin dieser neuartigen Gruppe, zeigt strukturelle Ähnlichkeiten und dient möglicherweise zur Erkennung einer Subpopulation von Pichia-Hefen. Im Rahmen dieser Arbeit konnten weiterhin drei epitheliale Adhäsine aus dem Humanpathogen Candida glabrata, Epa1A, Epa6A und Epa9A, strukturell und funktionell weitergehend untersucht werden. Dieser Subtyp der pilzlichen Adhäsine dient, unter Bindung von Galactosiden auf Epithelzellen, zur Etablierung der Pathogenität von C. glabrata. Durch die Lösung von Komplexstrukturen konnte gezeigt werden, dass eine funktionelle Klassifizierung nicht zwingend mit phylogenetischer Verwandtschaft einhergeht. Mit der strukturellen Untersuchung von Flo10A, einem Adhäsin des Flokkulin-Subtyps, welcher zur vegetativen Zellaggregation in Saccharomyces cerevisiae dient, konnte schließlich gezeigt werden, dass die Insertion von Subdomänen im Bereich der flexiblen Loops einen direkten Einfluss auf die Konformation der Bindungstasche und damit die Bindungseigenschaften hat.

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