Structures of pseudorabies virus capsids.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
22 03 2022
22 03 2022
Historique:
received:
21
07
2021
accepted:
02
03
2022
entrez:
23
3
2022
pubmed:
24
3
2022
medline:
13
4
2022
Statut:
epublish
Résumé
Pseudorabies virus (PRV) is a major etiological agent of swine infectious diseases and is responsible for significant economic losses in the swine industry. Recent data points to human viral encephalitis caused by PRV infection, suggesting that PRV may be able to overcome the species barrier to infect humans. To date, there is no available therapeutic for PRV infection. Here, we report the near-atomic structures of the PRV A-capsid and C-capsid, and illustrate the interaction that occurs between these subunits. We show that the C-capsid portal complex is decorated with capsid-associated tegument complexes. The PRV capsid structure is highly reminiscent of other α-herpesviruses, with some additional structural features of β- and γ-herpesviruses. These results illustrate the structure of the PRV capsid and elucidate the underlying assembly mechanism at the molecular level. This knowledge may be useful for the development of oncolytic agents or specific therapeutics against this arm of the herpesvirus family.
Identifiants
pubmed: 35318331
doi: 10.1038/s41467-022-29250-3
pii: 10.1038/s41467-022-29250-3
pmc: PMC8940892
doi:
Substances chimiques
Capsid Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1533Informations de copyright
© 2022. The Author(s).
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