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Evolution of virus-like architecture and packaging mechanisms in recycled bacterial proteins



A revolution in RNA packaging capsid

artificial nucleocapsid protein This could be similar to the proteins used by viruses to contain their genomes. It is a promising way to protect and deliver RNA, utilizing the challenge exacerbated by Tetter nucleases. and faculty Developed a multilayer globular cage-forming protein into a highly efficient capsid that selectively encoded its own RNA package. The cold-electron microscopy of the final design and the medium revealed stepped magnification. It is activated by destabilizing the amino acid substitution and domain exchange, which results in the alteration of the oligomerization interface for the cage base unit. In addition to protein changes Direct evolution also results in changes in the RNA coding structure that enable efficient uptake compared to RNA in other cells.

science, abg2822, this issue, p. 1

220.

Abstract

Viruses are the most prevalent pathogens around the world. With the assumption that their earliest progenitors recruited host proteins for virion formation, we used rigorous laboratory evolution to convert bacterial enzymes that lack affinity for nucleic acids to nucleocates. Efficiently packaged and protected multiple encoded copies of Messenger’s RNA. Revealing a remarkable convergence on the molecular quality mark of natural viruses. The simultaneous transformation reorganized the protein building blocks into a capsid icosahedral with 240 interlaced subunits that are impermeable to the nucleus. can cles And the emergence of durable RNA stem-loop cassettes ensures high yield and specificity. These findings also highlight practical strategies for developing non-viral vectors for a wide range of vaccines.


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