Virus self-assembly proceeds through contact-rich energy minima

Pedro Buzón, Sourav Maity, Panagiotis Christodoulis, Monique J Wiertsema, Steven Dunkelbarger, Christine Kim, Gijs J L Wuite, Adam Zlotnick, Wouter H Roos*

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

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Self-assembly of supramolecular complexes such as viral capsids occurs prominently in nature. Nonetheless, the mechanisms underlying these processes remain poorly understood. Here, we uncover the assembly pathway of hepatitis B virus (HBV), applying fluorescence optical tweezers and high-speed atomic force microscopy. This allows tracking the assembly process in real time with single-molecule resolution. Our results identify a specific, contact-rich pentameric arrangement of HBV capsid proteins as a key on-path assembly intermediate and reveal the energy balance of the self-assembly process. Real-time nucleic acid packaging experiments show that a free energy change of ~1.4 kBT per condensed nucleotide is used to drive protein oligomerization. The finding that HBV assembly occurs via contact-rich energy minima has implications for our understanding of the assembly of HBV and other viruses and also for the development of new antiviral strategies and the rational design of self-assembling nanomaterials.

Originele taal-2English
Artikelnummereabg0811
Aantal pagina's10
TijdschriftScience Advances
Volume7
Nummer van het tijdschrift45
DOI's
StatusPublished - 5-nov-2021

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