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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2021
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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. |
format | Online Article Text |
id | pubmed-8565845 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
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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