title: Assembly Pathway of Hepatitis B Core Virus-like Particles from Genetically Fused Dimers.
abstract: Macromolecular complexes are responsible for many key biological processes. However, in most cases details of the assembly/disassembly of such complexes are unknown at the molecular level, as the low abundance and transient nature of assembly intermediates make analysis challenging. The assembly of virus capsids is an example of such a process. The hepatitis B virus capsid (core) can be composed of either 90 or 120 dimers of coat protein. Previous studies have proposed a trimer of dimers as an important intermediate species in assembly, acting to nucleate further assembly by dimer addition. Using novel genetically-fused coat protein dimers, we have been able to trap higher-order assembly intermediates and to demonstrate for the first time that both dimeric and trimeric complexes are on pathway to virus-like particle (capsid) formation.
authors.affiliation: From the School of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom and.
authors.forename: Kris
authors.initials: K
authors.lastname: Holmes
authors.affiliation: From the School of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom and.
authors.forename: Dale A
authors.initials: DA
authors.lastname: Shepherd
authors.affiliation: From the School of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom and.
authors.forename: Alison E
authors.initials: AE
authors.lastname: Ashcroft
authors.affiliation: iQur Ltd, London Bioscience Innovation Centre, 2 Royal College Street, London NW1 0NH, United Kingdom.
authors.forename: Mike
authors.initials: M
authors.lastname: Whelan
authors.affiliation: From the School of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom and.
authors.forename: David J
authors.initials: DJ
authors.lastname: Rowlands
authors.affiliation: From the School of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom and n.j.stonehouse@leeds.ac.uk.
authors.forename: Nicola J
authors.initials: NJ
authors.lastname: Stonehouse
mesh_terms: D002213:Capsid / Q000737:chemistry / Q000378:metabolism; D036022:Capsid Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D019281:Dimerization; D006515:Hepatitis B virus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D008958:Models, Molecular; D014771:Virion / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D019065:Virus Assembly
chemical_list: D036022:Capsid Proteins
keywords: capsid; fused dimer; hepatitis virus; mass spectrometry (MS); protein assembly; protein self-assembly; tandem core; virus assembly