Insights into Paramyxovirus Nucleocapsids from Diverse Assemblies.
Paramyxoviridae
clam-shaped structure
double-headed nucleocapsids
nucleocapsid
nucleoprotein
Journal
Viruses
ISSN: 1999-4915
Titre abrégé: Viruses
Pays: Switzerland
ID NLM: 101509722
Informations de publication
Date de publication:
10 12 2021
10 12 2021
Historique:
received:
29
10
2021
revised:
29
11
2021
accepted:
07
12
2021
entrez:
28
12
2021
pubmed:
29
12
2021
medline:
1
2
2022
Statut:
epublish
Résumé
All paramyxoviruses, which include the mumps virus, measles virus, Nipah virus, Newcastle disease virus, and Sendai virus, have non-segmented single-stranded negative-sense RNA genomes. These RNA genomes are enwrapped throughout the viral life cycle by nucleoproteins, forming helical nucleocapsids. In addition to these helical structures, recombinant paramyxovirus nucleocapsids may occur in other assembly forms such as rings, clam-shaped structures, and double-headed nucleocapsids; the latter two are composed of two single-stranded helices packed in a back-to-back pattern. In all of these assemblies, the neighboring nucleoprotein protomers adopt the same domain-swapping mode via the N-terminal arm, C-terminal arm, and recently disclosed N-hole. An intrinsically disordered region in the C-terminal domain of the nucleoproteins, called the N-tail, plays an unexpected role in regulating the transition among the different assembly forms that occurs with other viral proteins, especially phosphoprotein. These structures, together with the helical nucleocapsids, significantly enrich the structural diversity of the paramyxovirus nucleocapsids and help explain the functions of these diverse assemblies, including RNA genome protection, transcription, and replication, as well as encapsulation.
Identifiants
pubmed: 34960748
pii: v13122479
doi: 10.3390/v13122479
pmc: PMC8705878
pii:
doi:
Substances chimiques
Nucleocapsid Proteins
0
Protein Subunits
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
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