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Título: | Cryo-electron microscopy for the study of virus assembly |
Autor: | Luque, Daniel; Castón, José R. | Palabras clave: | Chemical biology Structural biology Structure determination Virology |
Fecha de publicación: | mar-2020 | Editor: | Springer Nature | Citación: | Nature Chemical Biology 16: 231-239 (2020) | Resumen: | 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. | Versión del editor: | http://dx.doi.org/10.1038/s41589-020-0477-1 | URI: | http://hdl.handle.net/10261/228846 | DOI: | 10.1038/s41589-020-0477-1 | ISSN: | 1552-4450 | E-ISSN: | 1552-4469 |
Aparece en las colecciones: | (CNB) Artículos |
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accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
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