Please use this identifier to cite or link to this item: https://doi.org/10.21256/zhaw-21812
Publication type: Article in scientific journal
Type of review: Peer review (publication)
Title: Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain
Authors: 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
Published in: Journal of Structural Biology: X
Volume(Issue): 4
Pages: 100021
Issue Date: 29-Feb-2020
Publisher / Ed. Institution: Elsevier
ISSN: 2590-1524
Language: English
Subjects: 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
Subject (DDC): 579: Microbiology
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.
URI: https://digitalcollection.zhaw.ch/handle/11475/21812
Fulltext version: Published version
License (according to publishing contract): CC BY 4.0: Attribution 4.0 International
Departement: Life Sciences and Facility Management
Organisational Unit: Institute of Chemistry and Biotechnology (ICBT)
Appears in collections:Publikationen Life Sciences und Facility Management

Files in This Item:
File Description SizeFormat 
2020_Kalbermatter-et-al_Cryo-EM-structure.pdf3.04 MBAdobe PDFThumbnail
View/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.