Please use this identifier to cite or link to this item:
https://doi.org/10.21256/zhaw-21812
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kalbermatter, David | - |
dc.contributor.author | Shrestha, Neeta | - |
dc.contributor.author | Gall, Flavio | - |
dc.contributor.author | Wyss, Marianne | - |
dc.contributor.author | Riedl, Rainer | - |
dc.contributor.author | Plattet, Philippe | - |
dc.contributor.author | Fotiadis, Dimitrios | - |
dc.date.accessioned | 2021-02-18T13:38:54Z | - |
dc.date.available | 2021-02-18T13:38:54Z | - |
dc.date.issued | 2020-02-29 | - |
dc.identifier.issn | 2590-1524 | de_CH |
dc.identifier.uri | https://digitalcollection.zhaw.ch/handle/11475/21812 | - |
dc.description.abstract | 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. | de_CH |
dc.language.iso | en | de_CH |
dc.publisher | Elsevier | de_CH |
dc.relation.ispartof | Journal of Structural Biology: X | de_CH |
dc.rights | http://creativecommons.org/licenses/by/4.0/ | de_CH |
dc.subject | CDV, canine distemper virus | de_CH |
dc.subject | Canine distemper virus | de_CH |
dc.subject | Cryo-electron microscopy | de_CH |
dc.subject | FP, fusion peptide | de_CH |
dc.subject | Fusion protein | de_CH |
dc.subject | MeV, measles virus | de_CH |
dc.subject | Morbillivirus cell entry | de_CH |
dc.subject | Single particle reconstruction | de_CH |
dc.subject | cryo-EM, cryo-electron microscopy | de_CH |
dc.subject.ddc | 579: Mikrobiologie | de_CH |
dc.title | Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain | de_CH |
dc.type | Beitrag in wissenschaftlicher Zeitschrift | de_CH |
dcterms.type | Text | de_CH |
zhaw.departement | Life Sciences und Facility Management | de_CH |
zhaw.organisationalunit | Institut für Chemie und Biotechnologie (ICBT) | de_CH |
dc.identifier.doi | 10.1016/j.yjsbx.2020.100021 | de_CH |
dc.identifier.doi | 10.21256/zhaw-21812 | - |
dc.identifier.pmid | 32647825 | de_CH |
zhaw.funding.eu | No | de_CH |
zhaw.originated.zhaw | Yes | de_CH |
zhaw.pages.start | 100021 | de_CH |
zhaw.publication.status | publishedVersion | de_CH |
zhaw.volume | 4 | de_CH |
zhaw.publication.review | Peer review (Publikation) | de_CH |
zhaw.funding.snf | 183481 | de_CH |
zhaw.webfeed | CC Drug Discovery | de_CH |
zhaw.author.additional | No | de_CH |
zhaw.display.portrait | Yes | de_CH |
Appears in collections: | Publikationen Life Sciences und Facility Management |
Files in This Item:
File | Description | Size | Format | |
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2020_Kalbermatter-et-al_Cryo-EM-structure.pdf | 3.04 MB | Adobe PDF | View/Open |
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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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