Litcius/Paper detail

Cryo-EM reconstructions of BMV-derived virus-like particles reveal assembly defects in the icosahedral lattice structure

M. Ruszkowski, Aleksander Strugała, Paulina Indyka, Guillaume Tresset, Marek Figlerowicz, Anna Urbanowicz

2022Nanoscale20 citationsDOIOpen Access PDF

Abstract

from the recombinant capsid protein of brome mosaic virus (BMV). The analysis of VLPs was performed by Cryo-EM reconstructions and allowed us to visualize a few classes of VLPs, giving insight into the VLP self-assembly process. Apart from the mature icosahedral VLP practically identical with native virions, we describe putative VLP intermediates displaying non-icosahedral arrangements of capsomers, proposed to occur before the final disorder-order transition stage of icosahedral VLP assembly. Some of the described VLP classes show a lack of protein shell continuity, possibly resulting from too strong interaction with the cargo (in this case tRNA) with the capsid protein. We believe that our results are a useful prerequisite for the rational design of VLPs in the future and lead the way to the effective production of modified VLPs.

Topics & Concepts

Icosahedral symmetryCapsidCapsomereBrome mosaic virusVirus-like particleCrystallographyBiophysicsBiologyChemistryNanotechnologyRecombinant DNAVirusMaterials scienceVirologyPolymeraseBiochemistryDNARNA-dependent RNA polymeraseGeneBacteriophages and microbial interactionsPlant Virus Research StudiesViral gastroenteritis research and epidemiology
Cryo-EM reconstructions of BMV-derived virus-like particles reveal assembly defects in the icosahedral lattice structure | Litcius