Point mutation in a virus-like capsid drives symmetry reduction to form tetrahedral cages.
HK97
encapsulin
protein cage
self-assembly
viral capsid
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
14 May 2024
14 May 2024
Historique:
medline:
10
5
2024
pubmed:
10
5
2024
entrez:
9
5
2024
Statut:
ppublish
Résumé
Protein capsids are a widespread form of compartmentalization in nature. Icosahedral symmetry is ubiquitous in capsids derived from spherical viruses, as this geometry maximizes the internal volume that can be enclosed within. Despite the strong preference for icosahedral symmetry, we show that simple point mutations in a virus-like capsid can drive the assembly of unique symmetry-reduced structures. Starting with the encapsulin from
Identifiants
pubmed: 38722807
doi: 10.1073/pnas.2321260121
doi:
Substances chimiques
Capsid Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2321260121Subventions
Organisme : Wellcome Trust
ID : 110145
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 110146
Pays : United Kingdom
Déclaration de conflit d'intérêts
Competing interests statement:Two of the authors (B.E.D. and M.F.J.) are shareholders in Megadalton Solutions, a company that is engaged in commercializing CDMS. B.E.D. is an employee of Megadalton Solutions and M.F.J. is a consultant for Waters.