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  Cryo-EM structure of the cetacean morbillivirus nucleoprotein-RNA complex

Zinzula, L., Beck, F., Klumpe, S., Bohn, S., Pfeifer, G., Bollschweiler, D., et al. (2021). Cryo-EM structure of the cetacean morbillivirus nucleoprotein-RNA complex. Journal of Structural Biology, 213(3): 107750. doi:10.1016/j.jsb.2021.107750.

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 Creators:
Zinzula, Luca1, Author              
Beck, Florian1, Author              
Klumpe, Sven1, Author              
Bohn, Stefan1, Author              
Pfeifer, Günter1, Author              
Bollschweiler, Daniel2, Author              
Nagy, Istvan1, Author              
Plitzko, Jürgen M.1, Author              
Baumeister, Wolfgang1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              

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Free keywords: MEASLES-VIRUS; DOLPHIN MORBILLIVIRUS; ELECTRON-MICROSCOPY; NUCLEOCAPSID GENE; PROTEIN; SEQUENCE; GENOME; TRANSMISSION; INTERFACE; DYNAMICSBiochemistry & Molecular Biology; Biophysics; Cell Biology; Cetacean morbillivirus; Nucleocapsid; RNA virus replication; Cryo-electron microscopy; Helical reconstruction;
 Abstract: Cetacean morbillivirus (CeMV) is an emerging and highly infectious paramyxovirus that causes outbreaks in cetaceans and occasionally in pinnipeds, representing a major threat to biodiversity and conservation of endangered marine mammal populations in both hemispheres. As for all non-segmented, negative-sense, single stranded RNA (ssRNA) viruses, the morbilliviral genome is enwrapped by thousands of nucleoprotein (N) protomers. Each bound to six ribonucleotides, N protomers assemble to form a helical ribonucleoprotein (RNP) complex that serves as scaffold for nucleocapsid formation and as template for viral replication and transcription. While the molecular details on RNP complexes elucidated in human measles virus (MeV) served as paradigm model for these processes in all members of the Morbillivirus genus, no structural information has been obtained from other morbilliviruses, nor has any CeMV structure been solved so far. We report the structure of the CeMV RNP complex, reconstituted in vitro upon binding of recombinant CeMV N to poly-adenine ssRNA hexamers and solved to 4.0 A resolution by cryo-electron microscopy. In spite of the amino acid sequence similarity and consequently similar folding of the N protomer, the CeMV RNP complex exhibits different helical parameters as compared to previously reported MeV orthologs. The CeMV structure reveals exclusive interactions leading to more extensive protomer-RNA and protomer-protomer interfaces. We identified twelve residues, among those varying between CeMV strains, as putatively important for the stabilization of the RNP complex, which highlights the need to study the potential of CeMV N mutations that modulate nucleocapsid assembly to also affect viral phenotype and host adaptation.

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Language(s): eng - English
 Dates: 2021
 Publication Status: Published online
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000692069800001
DOI: 10.1016/j.jsb.2021.107750
 Degree: -

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Title: Journal of Structural Biology
  Abbreviation : J. Struct. Biol.
Source Genre: Journal
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Publ. Info: San Diego, CA : Elsevier
Pages: - Volume / Issue: 213 (3) Sequence Number: 107750 Start / End Page: - Identifier: ISSN: 1047-8477
CoNE: https://pure.mpg.de/cone/journals/resource/954922650160