Publikationsserver der Universitätsbibliothek Marburg
Titel:Einfluss gezielter Mutationen auf die biologische Aktivität des Oberflächen-Glykoproteins eines afrikanischen Henipavirus
Autor:Behner, Laura
Weitere Beteiligte: Maisner, Andrea (Prof. Dr.)
Veröffentlicht:2017
URI:https://archiv.ub.uni-marburg.de/diss/z2018/0097
URN: urn:nbn:de:hebis:04-z2018-00971
DOI: https://doi.org/10.17192/z2018.0097
DDC: Biowissenschaften, Biologie
Titel (trans.):Influence of specific mutations on the biological activity of an African henipavirus surface glycoprotein
Publikationsdatum:2018-10-15
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
Glykoprotein, Henipavirus, Oligomerisierung, Oligomerisierung, Fusionshelferfunktion, Oberflächenexpression, Oberflächenexpression, Henipavirus, Henipavirus, Fusionshelferfunktion, fusion-helper function, glycoprotein, surface expression, Glykoprotein, oligomerization

Zusammenfassung:
Hendra- und Nipahviren stellen die beiden hochpathogenen Vertreter des Genus Henipavirus dar. Ihr natürlicher Wirt sind Flughunde der Gattung Pteropus. Während die Infektion in Flughunden asymptomatisch verläuft, verursachen Henipaviren in Menschen und anderen Säugetieren, wie Schweinen oder Pferden, schwerwiegende Infektionen und gehören deshalb zu den sogenannten BSL-4 Erregern. Bis vor einigen Jahren ging man davon aus, dass das Vorkommen der Henipaviren auf Südostasien und Australien beschränkt ist. Inzwischen gibt es jedoch immer mehr Hinweise darauf, dass das Verbreitungsgebiet der Henipaviren deutlich größer ist. So wurden beispielsweise in Westafrika (Ghana) Henipavirus-ähnliche RNA-Sequenzen aus Flughunden der Spezies Eidolon helvum isoliert. Eines dieser afrikanischen Henipaviren, Kumasivirus (KV), konnte vollständig sequenziert werden. Da jedoch bis heute kein vermehrungsfähiges Virus aus Flughunden isoliert werden konnte, kann das zoonotische Potential neuer Henipaviren nur durch die funktionelle Charakterisierung einzelner viraler Proteine im Vergleich zu den homologen Proteinen bekannter humanpathogener Henipaviren abgeschätzt werden. Die beiden viralen Oberflächenproteine G und F sind für den Eintritt von Henipaviren in Wirtszellen und ihre Ausbreitung auf Nachbarzellen von zentraler Bedeutung. Nur wenn das G-Protein erfolgreich an seinen zellulären Rezeptor gebunden hat und seine sogenannte Fusionshelferfunktion ausübt, kann das F-Protein die Virus-Zell- oder die Zell-Zell-Fusion einleiten. Es konnte bereits gezeigt werden, dass die Oberflächenexpression und die Fusionshelferaktivität des KV-G Proteins im Vergleich zu anderen Henipavirus Glykoproteinen deutlich reduziert ist. Um die Ursache hierfür aufzuklären, wurde in dieser Arbeit das KV-G Protein im Vergleich zum G-Protein des pathogenen Nipahvirus (NiV-G) auf molekularer Ebene charakterisiert. Dafür wurden verschiedene Mutationen in das Protein eingefügt, die das N-Glykosylierungsmuster, die Oligomerisierung oder die Endozytose des Proteins beeinflussten. Western Blot Analysen, metabolische Markierungen sowie funktionelle Fusionsassays ergaben, dass das KV-G Protein, wie auch das NiV-G, sechs N-Glykane besitzt, die alle für den Oberflächentransport und die biologische Aktivität essentiell sind. Die Oligomerisierung des KV-G Proteins scheint sich jedoch von der des NiV-G Proteins zu unterscheiden. KV-G wird nicht in einem ausgewogenen Dimer-Tetramer-Verhältnis exprimiert, sondern bildet hauptsächlich hocholigomere Formen aus. Cystein-Mutationen in der Stieldomäne des KV-G Proteins führten zwar zu einer Veränderung des Oligomerisierungsmusters, allerdings konnte weder die Oberflächenexpression noch die Fusionshelferfunktion verbessert werden. Interessanterweise führte jedoch die Mutation eines nicht konservierten Cysteins in der Kopfdomäne zu einer signifikant gesteigerten Fusionshelferfunktion des KV-G Proteins. Die Aktivität konnte weiter gesteigert werden, wenn zusätzlich das Endozytose-Motiv in der zytoplasmatischen Domäne zerstört wurde. In dieser Arbeit konnte zum ersten Mal eine signifikant gesteigerte Aktivität (gain of function) eines Glykoproteins eines afrikanischen Henipavirus nachgewiesen werden. Auch wenn die biologische Aktivität des KV-G Proteins im Vergleich zu Glykoproteinen hochpathogener Henipaviren immer noch stark eingeschränkt ist, muss davon ausgegangen werden, dass durch wenige adaptive Punktmutationen afrikanische Henipaviren mit gesteigerter Funktion und damit eventuell höherem zoonotischen Potential entstehen können.

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