A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.
T number
actinobacteriophage
bacteriophage
capsid
cryo-EM
isopeptide bond
structural phylogenetics
tailed bacteriophage
Journal
Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697
Informations de publication
Date de publication:
02 03 2023
02 03 2023
Historique:
received:
13
09
2022
revised:
31
10
2022
accepted:
19
12
2022
pmc-release:
02
03
2024
pubmed:
18
1
2023
medline:
8
3
2023
entrez:
17
1
2023
Statut:
ppublish
Résumé
Many double-stranded DNA viruses, including tailed bacteriophages (phages) and herpesviruses, use the HK97-fold in their major capsid protein to make the capsomers of the icosahedral viral capsid. After the genome packaging at near-crystalline densities, the capsid is subjected to a major expansion and stabilization step that allows it to withstand environmental stresses and internal high pressure. Several different mechanisms for stabilizing the capsid have been structurally characterized, but how these mechanisms have evolved is still not understood. Using cryo-EM structure determination of 10 capsids, structural comparisons, phylogenetic analyses, and Alphafold predictions, we have constructed a detailed structural dendrogram describing the evolution of capsid structural stability within the actinobacteriophages. We show that the actinobacteriophage major capsid proteins can be classified into 15 groups based upon their HK97-fold.
Identifiants
pubmed: 36649709
pii: S0969-2126(22)00498-1
doi: 10.1016/j.str.2022.12.012
pmc: PMC10071307
mid: NIHMS1861238
pii:
doi:
Substances chimiques
Capsid Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
282-294.e5Subventions
Organisme : Howard Hughes Medical Institute
ID : GT12053
Pays : United States
Organisme : NIH HHS
ID : S10 OD019995
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM131729
Pays : United States
Organisme : NIGMS NIH HHS
ID : U24 GM129547
Pays : United States
Organisme : NIH HHS
ID : S10 OD025009
Pays : United States
Informations de copyright
Copyright © 2022 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests G.F.H. is a compensated consultant for Tessera and for Janssen Inc. The remaining authors declare no competing interests.
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