Exit of simian virus 40 from the endoplasmic reticulum
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1 Research Collection Doctoral Thesis Exit of simian virus 40 from the endoplasmic reticulum Author(s): Geiger, Roger Publication Date: 2011 Permanent Link: Rights / License: In Copyright - Non-Commercial Use Permitted This page was generated automatically upon download from the ETH Zurich Research Collection. For more information please consult the Terms of use. ETH Library
2 DISS. ETH NO Exit of Simian Virus 40 from the Endoplasmic Reticulum A dissertation submitted to ETH Zurich for the degree of Doctor of Sciences presented by Roger Geiger Dipl. Natw. ETH, ETH Zürich born September 2 nd, 1980 citizen of Winterthur and Bischofszell accepted on the recommendation of Prof. Dr. Ari Helenius, examiner Prof. Dr. Urs Greber, co- examiner Prof. Dr. Maurizio Molinari, co- examiner 2011
3 Summary Simian Virus 40 (SV40) is a member of the polyomaviruses. This is a family of small nonenveloped DNA viruses some of which are human pathogens. To infect cells, SV40 binds to the ganglioside GM1 at the plasma membrane, and after internalization it is transported to the lumen of the endoplasmic reticulum (ER). The ER provides a unique environment in which the highly stable virus capsid undergoes initial uncoating (destabilization) steps. To finally deliver its genome to the nucleus, the virus must overcome the membrane of the ER and reach the cytosol containing nuclear import factors. How the virus crosses the ER membrane is not understood and is the subject of the present thesis. Viruses that reached the ER appeared smaller in electron micrographs and exhibited electron dense protrusions pointing towards the ER membrane. Biochemical analysis revealed that these protrusions most likely correspond to the N- termini of a previously hidden minor structural protein VP2 that is exposed in the ER. Upon association with the ER membrane, the N- terminal peptide takes on an alpha- helical conformation and inserts into the membrane. It contains a negatively charged residue (Glu17), which is recognized as a degradation signal of misfolded or incompletely assembled membrane proteins by the ER associated degradation (ERAD) machinery. Using a sirna- mediated screen for infectivity, the ERAD components involved in recognition of the peptide were identified. These are Bap31 and two associated components, Bap29 and RMA1. Bap31 co- localizes with the virus in the ER and recognizes the N- terminal peptide of VP2 via charge pair interactions. These findings suggest that SV40 undergoes a conformational change in the ER leading to exposure and membrane insertion of the N- terminus of VP2. A specific ERAD machinery reserved for the degradation of misfolded membrane proteins 4
4 recognizes this peptide and presumably assists dislocation of the viral particle from the ER to the cytosol. 5
5 Zusammenfassung Das Simian Virus 40 (SV40) gehört zu den Polyomaviren. Dies ist eine Familie von kleinen, nicht- behüllten Viren zu der auch einige humane Pathogene zählen. Um Zellen zu infizieren bindet SV40 an GM1, ein Gangliosid in der Plasma Membran. Nach erfolgter Zell- Internalisierung wird das Virus ins endoplasmatische Retikulum (ER) transportiert. Das ER bietet eine Umgebung in der das äusserst stabile virale Kapsid destabilisiert wird. Um letzten Endes das Genom in den Nukleus zu bringen muss das Virus die Membran des ER überwinden und ins Zytosol gelangen welches nukleäre Importfaktoren enthält. Viren die das ER erreicht haben erscheinen kleiner in Elektronmikrographen und weisen in Richtung ER Membran Ausstülpungen auf. Biochemische Analysen zeigten dass diese Ausstülpungen höchst wahrscheinlich N- Termini des viralen Proteins VP2 sind. VP2 befindet sich innerhalb des viralen Kapsids und wird erst im ER exponiert. Sobald dieses Peptid mit der ER Membran in Kontakt kommt, nimmt es eine alpha- helikale Struktur an und inseriert in die Membran. Es enthält eine negativ geladene Aminosäure (Glu17) die in der ER Membran durch die ER assoziierte Degradations- (ERAD) Maschinerie als ein Degradationsignal von falsch gefalteten oder nicht komplett oliogmerisierten Proteinen erkannt wird. Durch einen sirna- screen wurden ERAD Komponenten identifiziert die in der Erkennung des Peptids involviert sind. Diese sind Bap31, Bap29 und RMA1. Diese Proteine interagieren miteinander in der ER- Membran. Bap31 kolokalisiert mit dem Virus im ER und erkennt das N- terminale Peptid von VP2 durch Ladugspaare. Diese Erkenntnisse suggerieren dass SV40 im ER eine strukturelle Änderung erfährt woraufhin das N- terminale Peptid von VP2 exponiert wird und anschliessend in die ER- Membran inseriert. Eine spezifische Maschinerie die für die Degradation von 6
6 falsch gefalteten Membranproteinen vorgesehen ist, erkennt das Peptid und assistiert vermutlich die Dislokation von dem Viruspartikel vom ER ins Zytoplasma. 7
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Research Collection Doctoral Thesis Studies on Pro-Environmental Behavior Future Orientation as a Predictor of Pro-Environmental Behavior and the Assessment of Ecological Impact Author(s): Bruderer Enzler,
Solution structure of the potential splicing factor RBMY in complex with an RNA stem-ioop
Doctoral Thesis ETH No. 16262 Solution structure of the potential splicing factor RBMY in complex with an RNA stem-ioop A dissertation submitted to the Swiss Federal Institute oftechnology Zurich for the
HPLC-Charakterisierung von Lektinen der Mistel (Viscum album L.) und Verbreitung der Pflanze in der Schweiz
Research Collection Doctoral Thesis HPLC-Charakterisierung von Lektinen der Mistel (Viscum album L.) und Verbreitung der Pflanze in der Schweiz Author(s): Hofstetter, Martin Publication Date: 1985 Permanent
Phosphorylation of IQGAP1 modulates its binding to Cdc42 revealing a new type of Rho-GTPase regulator
Research Collection Doctoral Thesis Phosphorylation of IQGAP1 modulates its binding to Cdc42 revealing a new type of Rho-GTPase regulator Author(s): Grohmanova, Katarina Publication Date: 2004 Permanent
Ueber die Cohomologie der Abbildungsklassengruppe
Research Collection Doctoral Thesis Ueber die Cohomologie der Abbildungsklassengruppe Author(s): Kaufmann, Manfred Publication Date: 1988 Permanent Link: https://doi.org/10.3929/ethz-a-000579619 Rights
Dopant clustering and diffusion in silicon
Research Collection Doctoral Thesis Dopant clustering and diffusion in silicon Author(s): Vollenweider, Kilian Publication Date: 2010 Permanent Link: https://doi.org/10.3929/ethz-a-006192842 Rights / License:
Binary adder architectures for cell-based VLSI and their synthesis
Research Collection Doctoral Thesis Binary adder architectures for cell-based VLSI and their synthesis Author(s): Zimmermann, Reto Publication Date: 1997 Permanent Link: https://doi.org/10.3929/ethz-a-001912749
Sterilisation von stückigen Lebensmitteln mit Mikrowellen
Research Collection Doctoral Thesis Sterilisation von stückigen Lebensmitteln mit Mikrowellen Author(s): Spreng, Hans Publication Date: 1975 Permanent Link: https://doi.org/10.3929/ethza000119193 Rights
Geometric Change Detection and Image Registration in Large Scale Urban Environments
Research Collection Doctoral Thesis Geometric Change Detection and Image Registration in Large Scale Urban Environments Author(s): Taneja, Aparna Publication Date: 2014 Permanent Link: https://doi.org/10.3929/ethz-a-010394826
Specification and enforcement in distributed usage control
Research Collection Doctoral Thesis Specification and enforcement in distributed usage control Author(s): Hilty, Manuel Publication Date: 2007 Permanent Link: https://doi.org/10.3929/ethz-a-005537428 Rights
Combining Lock-Free Programming with Cooperative Multitasking for a Portable Multiprocessor Runtime System
Research Collection Doctoral Thesis Combining Lock-Free Programming with Cooperative Multitasking for a Portable Multiprocessor Runtime System Author(s): Negele, Florian Publication Date: 2014 Permanent
Research Collection. Identification of imprinted genes and their functional roles in Arabidopsis thaliana. Doctoral Thesis.
Research Collection Doctoral Thesis Identification of imprinted genes and their functional roles in Arabidopsis thaliana Author(s): Wolff, Philip Publication Date: 2015 Permanent Link: https://doi.org/10.3929/ethz-a-010482475