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Publikationstyp: Beitrag in wissenschaftlicher Zeitschrift
Art der Begutachtung: Peer review (Publikation)
Titel: Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain
Autor/-in: Kalbermatter, David
Shrestha, Neeta
Gall, Flavio
Wyss, Marianne
Riedl, Rainer
Plattet, Philippe
Fotiadis, Dimitrios
et. al: No
DOI: 10.1016/j.yjsbx.2020.100021
10.21256/zhaw-21812
Erschienen in: Journal of Structural Biology: X
Band(Heft): 4
Seite(n): 100021
Erscheinungsdatum: 29-Feb-2020
Verlag / Hrsg. Institution: Elsevier
ISSN: 2590-1524
Sprache: Englisch
Schlagwörter: CDV, canine distemper virus; Canine distemper virus; Cryo-electron microscopy; FP, fusion peptide; Fusion protein; MeV, measles virus; Morbillivirus cell entry; Single particle reconstruction; cryo-EM, cryo-electron microscopy
Fachgebiet (DDC): 579: Mikrobiologie
Zusammenfassung: Measles virus (MeV) and canine distemper virus (CDV), two members of the Morbillivirus genus, are still causing important global diseases of humans and animals, respectively. To enter target cells, morbilliviruses rely on an envelope-anchored machinery, which is composed of two interacting glycoproteins: a tetrameric receptor binding (H) protein and a trimeric fusion (F) protein. To execute membrane fusion, the F protein initially adopts a metastable, prefusion state that refolds into a highly stable postfusion conformation as the result of a finely coordinated activation process mediated by the H protein. Here, we employed cryo-electron microscopy (cryo-EM) and single particle reconstruction to elucidate the structure of the prefusion state of the CDV F protein ectodomain (solF) at 4.3 Å resolution. Stabilization of the prefusion solF trimer was achieved by fusing the GCNt trimerization sequence at the C-terminal protein region, and expressing and purifying the recombinant protein in the presence of a morbilliviral fusion inhibitor class compound. The three-dimensional cryo-EM map of prefusion CDV solF in complex with the inhibitor clearly shows density for the ligand at the protein binding site suggesting common mechanisms of membrane fusion activation and inhibition employed by different morbillivirus members.
URI: https://digitalcollection.zhaw.ch/handle/11475/21812
Volltext Version: Publizierte Version
Lizenz (gemäss Verlagsvertrag): CC BY 4.0: Namensnennung 4.0 International
Departement: Life Sciences und Facility Management
Organisationseinheit: Institut für Chemie und Biotechnologie (ICBT)
Enthalten in den Sammlungen:Publikationen Life Sciences und Facility Management

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Kalbermatter, D., Shrestha, N., Gall, F., Wyss, M., Riedl, R., Plattet, P., & Fotiadis, D. (2020). Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain. Journal of Structural Biology: X, 4, 100021. https://doi.org/10.1016/j.yjsbx.2020.100021
Kalbermatter, D. et al. (2020) ‘Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain’, Journal of Structural Biology: X, 4, p. 100021. Available at: https://doi.org/10.1016/j.yjsbx.2020.100021.
D. Kalbermatter et al., “Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain,” Journal of Structural Biology: X, vol. 4, p. 100021, Feb. 2020, doi: 10.1016/j.yjsbx.2020.100021.
KALBERMATTER, David, Neeta SHRESTHA, Flavio GALL, Marianne WYSS, Rainer RIEDL, Philippe PLATTET und Dimitrios FOTIADIS, 2020. Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain. Journal of Structural Biology: X. 29 Februar 2020. Bd. 4, S. 100021. DOI 10.1016/j.yjsbx.2020.100021
Kalbermatter, David, Neeta Shrestha, Flavio Gall, Marianne Wyss, Rainer Riedl, Philippe Plattet, and Dimitrios Fotiadis. 2020. “Cryo-EM Structure of the Prefusion State of Canine Distemper Virus Fusion Protein Ectodomain.” Journal of Structural Biology: X 4 (February): 100021. https://doi.org/10.1016/j.yjsbx.2020.100021.
Kalbermatter, David, et al. “Cryo-EM Structure of the Prefusion State of Canine Distemper Virus Fusion Protein Ectodomain.” Journal of Structural Biology: X, vol. 4, Feb. 2020, p. 100021, https://doi.org/10.1016/j.yjsbx.2020.100021.


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