Atomic structure of a nudivirus occlusion body protein determined from a 70-year-old crystal sample.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
13 07 2023
13 07 2023
Historique:
received:
28
01
2023
accepted:
29
06
2023
medline:
17
7
2023
pubmed:
14
7
2023
entrez:
13
7
2023
Statut:
epublish
Résumé
Infectious protein crystals are an essential part of the viral lifecycle for double-stranded DNA Baculoviridae and double-stranded RNA cypoviruses. These viral protein crystals, termed occlusion bodies or polyhedra, are dense protein assemblies that form a crystalline array, encasing newly formed virions. Here, using X-ray crystallography we determine the structure of a polyhedrin from Nudiviridae. This double-stranded DNA virus family is a sister-group to the baculoviruses, whose members were thought to lack occlusion bodies. The 70-year-old sample contains a well-ordered lattice formed by a predominantly α-helical building block that assembles into a dense, highly interconnected protein crystal. The lattice is maintained by extensive hydrophobic and electrostatic interactions, disulfide bonds, and domain switching. The resulting lattice is resistant to most environmental stresses. Comparison of this structure to baculovirus or cypovirus polyhedra shows a distinct protein structure, crystal space group, and unit cell dimensions, however, all polyhedra utilise common principles of occlusion body assembly.
Identifiants
pubmed: 37443157
doi: 10.1038/s41467-023-39819-1
pii: 10.1038/s41467-023-39819-1
pmc: PMC10345106
doi:
Substances chimiques
Viral Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4160Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 200835/Z/16/Z
Pays : United Kingdom
Informations de copyright
© 2023. The Author(s).
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