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Virus self-assembly proceeds through contact-rich energy minima

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 atomi...

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Autores principales: Buzón, Pedro, Maity, Sourav, Christodoulis, Panagiotis, Wiertsema, Monique J., Dunkelbarger, Steven, Kim, Christine, Wuite, Gijs J.L., Zlotnick, Adam, Roos, Wouter H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8565845/
https://www.ncbi.nlm.nih.gov/pubmed/34730996
http://dx.doi.org/10.1126/sciadv.abg0811
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author Buzón, Pedro
Maity, Sourav
Christodoulis, Panagiotis
Wiertsema, Monique J.
Dunkelbarger, Steven
Kim, Christine
Wuite, Gijs J.L.
Zlotnick, Adam
Roos, Wouter H.
author_facet Buzón, Pedro
Maity, Sourav
Christodoulis, Panagiotis
Wiertsema, Monique J.
Dunkelbarger, Steven
Kim, Christine
Wuite, Gijs J.L.
Zlotnick, Adam
Roos, Wouter H.
author_sort Buzón, Pedro
collection PubMed
description 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 k(B)T 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.
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spelling pubmed-85658452021-11-17 Virus self-assembly proceeds through contact-rich energy minima Buzón, Pedro Maity, Sourav Christodoulis, Panagiotis Wiertsema, Monique J. Dunkelbarger, Steven Kim, Christine Wuite, Gijs J.L. Zlotnick, Adam Roos, Wouter H. Sci Adv Physical and Materials Sciences 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 k(B)T 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. American Association for the Advancement of Science 2021-11-03 /pmc/articles/PMC8565845/ /pubmed/34730996 http://dx.doi.org/10.1126/sciadv.abg0811 Text en Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.
spellingShingle Physical and Materials Sciences
Buzón, Pedro
Maity, Sourav
Christodoulis, Panagiotis
Wiertsema, Monique J.
Dunkelbarger, Steven
Kim, Christine
Wuite, Gijs J.L.
Zlotnick, Adam
Roos, Wouter H.
Virus self-assembly proceeds through contact-rich energy minima
title Virus self-assembly proceeds through contact-rich energy minima
title_full Virus self-assembly proceeds through contact-rich energy minima
title_fullStr Virus self-assembly proceeds through contact-rich energy minima
title_full_unstemmed Virus self-assembly proceeds through contact-rich energy minima
title_short Virus self-assembly proceeds through contact-rich energy minima
title_sort virus self-assembly proceeds through contact-rich energy minima
topic Physical and Materials Sciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8565845/
https://www.ncbi.nlm.nih.gov/pubmed/34730996
http://dx.doi.org/10.1126/sciadv.abg0811
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