Virus self-assembly proceeds through contact-rich energy minima.
Virus self-assembly proceeds through contact-rich energy minima.
复制标题
病毒自组装通过富含接触的能量最小值进行。
DOI:
10.1126/sciadv.abg0811
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发表时间:
2021-11-05
期刊:
影响因子:
13.6
通讯作者:
Roos WH
中科院分区:
文献类型:
--
作者:
Buzón P;Maity S;Christodoulis P;Wiertsema MJ;Dunkelbarger S;Kim C;Wuite GJL;Zlotnick A;Roos WH
Single-molecule fluorescence optical tweezers studies combined with high-speed AFM reveal early events in the HBV life cycle. 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.
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