AI Article Synopsis
- The assembly pathways of viral particles, including nucleation and genome compaction, remain largely unknown despite detailed understanding of their structures.
- Using advanced techniques like fluorescence optical tweezers, researchers studied how artificial capsid polypeptides form rod-shaped viruslike particles (VLPs).
- The findings reveal that small oligomers move along DNA, while larger ones stabilize VLP growth, indicating DNA is compacted through organized helical wrapping, which enhances understanding of viral assembly processes.
Article Abstract
While the structure of a multitude of viral particles has been resolved to atomistic detail, their assembly pathways remain largely elusive. Key unresolved issues are particle nucleation, particle growth, and the mode of genome compaction. These issues are difficult to address in bulk approaches and are effectively only accessible by the real-time tracking of assembly dynamics of individual particles. This we do here by studying the assembly into rod-shaped viruslike particles (VLPs) of artificial capsid polypeptides. Using fluorescence optical tweezers, we establish that small oligomers perform one-dimensional diffusion along the DNA. Larger oligomers are immobile and nucleate VLP growth. A multiplexed acoustic force spectroscopy approach reveals that DNA is compacted in regular steps, suggesting packaging via helical wrapping into a nucleocapsid. By reporting how real-time assembly tracking elucidates viral nucleation and growth principles, our work opens the door to a fundamental understanding of the complex assembly pathways of both VLPs and naturally evolved viruses.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6696885 | PMC |
| http://dx.doi.org/10.1021/acs.nanolett.9b02376 | DOI Listing |
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