Microbiology
Assembly Pathway of Hepatitis B Core Virus-like Particles from Genetically Fused Dimers*

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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.

hepatitis virus
mass spectrometry (MS)
protein assembly
protein self-assembly
virus assembly
capsid
fused dimer
tandem core

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*

This work was supported by an EPSRC White Rose studentship (to D. A. S.) and a Biotechnology and Biological Sciences Research Council CASE award (iQur PLC) (to K. H.). The authors declare that they have no conflicts of interest with the contents of this article.