Dokument: Die Rolle des LIPP Proteins in einer Chlamydia pneumoniae Infektion
| Titel: | Die Rolle des LIPP Proteins in einer Chlamydia pneumoniae Infektion | |||||||
| Weiterer Titel: | Role of the LIPP protein during infection by Chlamydia pneumoniae” | |||||||
| URL für Lesezeichen: | https://docserv.uni-duesseldorf.de/servlets/DocumentServlet?id=44654 | |||||||
| URN (NBN): | urn:nbn:de:hbz:061-20180117-135211-5 | |||||||
| Kollektion: | Dissertationen | |||||||
| Sprache: | Deutsch | |||||||
| Dokumententyp: | Wissenschaftliche Abschlussarbeiten » Dissertation | |||||||
| Medientyp: | Text | |||||||
| Autor: | M. Sc. Galle, Jan Niklas [Autor] | |||||||
| Dateien: |
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| Beitragende: | Prof. Dr. Hegemann, J. H. [Betreuer/Doktorvater] Prof. Dr. Hegemann, J. H. [Gutachter] Prof. Dr. Lutz Schmitt [Gutachter] | |||||||
| Stichwörter: | Chlamydia pneumoniae, Phosphatidylserin, Lipide, Cholesterin, Lipid-Translokation, Infektion, Internalisierung | |||||||
| Dewey Dezimal-Klassifikation: | 500 Naturwissenschaften und Mathematik » 570 Biowissenschaften; Biologie | |||||||
| Beschreibungen: | Für das Gram-negative, obligat intrazelluläre Pathogen Chlamydia pneumoniae (C. pn.) sind Adhäsion und die darauffolgende Internalisierung die ersten essentiellen Schritte im Infektionszyklus. Neben dem Außenmembran-Protein OmcB, welches an Glykosaminoglykane bindet, und dem Polymorphen Membran-Protein 21 (Pmp21), welches mit dem humanen EGF-Rezeptor (EGFR) interagiert, konnte CPn0473 als weiteres C. pn.-spezifisches Adhäsin identifiziert werden. Interessanterweise stimuliert rekombinantes CPn0473 (rCPn0473) Dosis-abhängig die chlamydiale Internalisierung über einen unbekannten Mechanismus. Die Bindung des Proteins an die Humanzelle erfolgt über eine 50 Aminosäuren (AS) lange Bindedomäne im C-Terminus, während die Stimulation der Internalisierung durch eine 150 AS lange Domäne im N-Terminus vermittelt wird. In dieser Arbeit sollte das Protein CPn0473 im Detail studiert und seine Rolle während der Adhäsion und Internalisierung von C. pn. aufgeklärt werden.
Bindeassays an Proteinase K-vorbehandelten Humanzellen zeigten, dass der erste Kontakt von rCPn0473 mit Oberflächenproteinen der Wirtszelle erfolgt. Das Protein integriert daraufhin über eine Transmembrandomäne (TM) im C-Terminus (AS 396-426) in die humane Plasmamembran (PM). Diese Domäne ist auch für die Interaktion des Proteins mit anderen rCPn0473-Proteinen essentiell. Durch konfokale Mikroskopie konnte gezeigt werden, dass sowohl Chlamydien als auch rCPn0473 das negativ-geladene Lipid Phosphatidylserin (PS), welches auf der inneren Seite der humanen PM lokalisiert ist, in Cholesterin-reichen Regionen zu externalisieren. Die Humanzellen zeigten dabei kein Anzeichen einer Induktion der Apoptose. CPn0473 bindet spezifisch an PS-haltige Giant unilamellar vesicles (GUVs). Die PS-Translokation an der humanen Zelle und die Bindung des Lipids werden dabei durch die gleiche CPn0473Domäne vermittelt, die auch für die Stimulation der chlamydialen Internalisierung verantwortlich ist. Eine Erhöhung der CPn0473-Moleküle auf der chlamydialen EB Oberfläche durch mit rCPn0473 erhöhte in der folgenden Infektion die PS-Translokation an der humanen PM. Darüber hinaus konnte in Experimenten mit asymmetrischen GUVs gezeigt werden, dass die Bindung von rCPn0473 die PS-Translokation vermittelt. Zusammenfassend konnte in dieser Arbeit ein neuer Mechanismus der chlamydialen Internalisierung identifiziert werden. CPn0473 ist dabei das erste Protein, welches von der extrazellulären Seite an die PM einer Wirtszelle bindet und die Translokation eines Lipids induziert.For the Gram-negative, obligate intracellular pathogen Chlamydia pneumoniae (C. pn.) adhesion and subsequent internalization into the host cell is essential for the progression of the infection cycle. C. pn. adheres via the OmcB to heparan sulfate moieties, while Pmp21 binds and activates the human EGF receptor. Recently, CPn0473 was identified as an additional C. pn.-specific adhesin located on the surface of infectious EBs. In contrast to classical adhesins, pre-incubation of human cells with recombinant CPn0473 (rCPn0473) prior to an infection does not lead to a reduced infectivity but rather boosts chlamydial internalization. Binding to the host cell is realized by a 50 aa long binding-domain in the C-Terminus, while the infection boost is accomplished by a 150 aa long N-terminal CPn0473 domain. This study aimed to investigate the protein CPn0473 in more detail and elucidate its role in the chlamydial adhesion and internalization processes. Binding assays with Proteinase K-treated human cells suggested that the first contact of CPn0473 with the human cell is fulfilled by binding to a protein or protein-associated molecule on the human cell surface. Bound to the host PM, rCPn0473 penetrates the host plasma membrane (PM) via a C-terminal transmembrane domain (TM). The same domain is essential for an observed self-interaction of the protein. Microscopic analysis showed that rCPn0473 then induces externalization of the negatively-charged phospholipid phosphatidylserine (PS) in cholesterol-enriched liquid ordered phases of the PM. Classical apoptotic markers in the host cell were not activated during this process. In GUV binding assays, lipid binding by rCPn0473 occurred via the infection-enhancing, N-terminal CPn0473 domain. PS, usually restricted to the inner leaflet of the PM, became externalized within minutes after adhesion of C. pn. An increase of accessible CPn0473 by coating of chlamydial EBs with rCPn0473 prior to an infection increased infectivity and the rate of externalization dose-dependently. A reduced level of PS in the host cell diminished rCPn0473-induced internalization of C. pn. and PS externalization. Importantly, incubation of rCPn0473 with asymmetric GUVs indicated, that CPn0473 itself is able to externalize PS without help of additional proteins. Overall, the data show that CPn0473 is able to bind and externalize PS in the host PM in order to promote the uptakes of C. pn. By that, CPn0473 is the first bacterial protein which binds to the extracellular leaflet of the host cell in order to translocate host cell phospholipids. | |||||||
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| Lizenz: |  Urheberrechtsschutz | |||||||
| Fachbereich / Einrichtung: | Mathematisch- Naturwissenschaftliche Fakultät » WE Biologie » Funktionelle Genomforschung der Mikroorganismen | |||||||
| Dokument erstellt am: | 17.01.2018 | |||||||
| Dateien geändert am: | 17.01.2018 | |||||||
| Promotionsantrag am: | 13.03.2014 | |||||||
| Datum der Promotion: | 20.12.2017 |
