期刊
NATURE CHEMICAL BIOLOGY
卷 16, 期 3, 页码 231-239出版社
NATURE RESEARCH
DOI: 10.1038/s41589-020-0477-1
关键词
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资金
- Spanish Ministry of Economy and Competitivity [BFU2017-88736-R]
- Comunidad Autonoma de Madrid [P2018/NMT-4389]
Although viruses are extremely diverse in shape and size, evolution has led to a limited number of viral classes or lineages, which is probably linked to the assembly constraints of a viable capsid. Viral assembly mechanisms are restricted to two general pathways, (i) co-assembly of capsid proteins and single-stranded nucleic acids and (ii) a sequential mechanism in which scaffolding-mediated capsid precursor assembly is followed by genome packaging. Cryo-electron microscopy (cryo-EM) and cryo-electron tomography (cryo-ET), which are revolutionizing structural biology, are central to determining the high-resolution structures of many viral assemblies as well as those of assembly intermediates. This wealth of cryo-EM data has also led to the development and redesign of virus-based platforms for biomedical and biotechnological applications. In this Review, we will discuss recent viral assembly analyses by cryo-EM and cryo-ET showing how natural assembly mechanisms are used to encapsulate heterologous cargos including chemicals, enzymes, and/or nucleic acids for a variety of nanotechnological applications. Cryo-EM and Cryo-ET have emerged as useful tools to study the efficient and dynamic processes of the viral assembly.
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