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Title | Cryo-EM reconstructions of BMV-derived virus-like particles reveal assembly defects in the icosahedral lattice structure. |
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Journal, issue, pages | Nanoscale, Vol. 14, Issue 8, Page 3224-3233, Year 2022 |
Publish date | Feb 24, 2022 |
Authors | Milosz Ruszkowski / Aleksander Strugala / Paulina Indyka / Guillaume Tresset / Marek Figlerowicz / Anna Urbanowicz / |
PubMed Abstract | The increasing interest in virus-like particles (VLPs) has been reflected by the growing number of studies on their assembly and application. However, the formation of complete VLPs is a complex ...The increasing interest in virus-like particles (VLPs) has been reflected by the growing number of studies on their assembly and application. However, the formation of complete VLPs is a complex phenomenon, making it difficult to rationally design VLPs with desired features . In this paper, we describe VLPs assembled 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. |
External links | Nanoscale / PubMed:35156989 |
Methods | EM (single particle) |
Resolution | 3.0 - 3.2 Å |
Structure data | EMDB-13344, PDB-7pe1: EMDB-13345, PDB-7pe2: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | VIRUS LIKE PARTICLE / BMV / brome mosaic virus / capsid proteins |