Single-particle studies of the effects of RNA-protein interactions on the self-assembly of RNA virus particles.

ABSTRACT: Understanding the pathways by which simple RNA viruses self-assemble from their coat proteins and RNA is of practical and fundamental interest. Although RNA-protein interactions are thought to play a critical role in the assembly, our understanding of their effects is limited because the assembly process is difficult to observe directly. We address this problem by using interferometric scattering microscopy, a sensitive optical technique with high dynamic range, to follow the in vitro assembly kinetics of more than 500 individual particles of brome mosaic virus (BMV)-for which RNA-protein interactions can be controlled by varying the ionic strength of the buffer. We find that when RNA-protein interactions are weak, BMV assembles by a nucleation-and-growth pathway in which a small cluster o

SUBMITTER: Garmann RF 

PROVIDER: S-EPMC9522328 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature