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Related Experiment Video

Updated: Nov 28, 2025

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly

Published on: March 1, 2012

Virus Assembly Pathways: Straying Away but Not Too Far.

Kevin Bond¹, Irina B Tsvetkova¹, Joseph Che-Yen Wang²

¹Department of Chemistry, Indiana University, Bloomington, IN, 47405, USA.

Small (Weinheim an Der Bergstrasse, Germany)

|November 26, 2020

Summary

Researchers discovered novel, unstable virus-like particles formed by brome mosaic virus (BMV) coat proteins and RNA. These structures can be recycled into infectious virions, suggesting a new viral RNA packaging pathway.

Keywords:

brome mosaic virus charge detection mass spectrometry cryo-electron microcopy virus assembly

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Last Updated: Nov 28, 2025

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Combining Analysis of DNA in a Crude Virion Extraction with the Analysis of RNA from Infected Leaves to Discover New Virus Genomes

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Published on: July 27, 2018

Area of Science:

Virology
Structural Biology
Molecular Biology

Background:

Non-enveloped RNA viruses assemble viral RNA with capsid proteins within host cells.
In vitro studies show virus-like particles can package non-viral polyanionic molecules, posing a puzzle for in vivo viral RNA selection.
The precise mechanism of selective viral RNA packaging remains incompletely understood.

Purpose of the Study:

To investigate the in vitro assembly of brome mosaic virus (BMV) coat proteins with nucleic acid oligomers.
To elucidate the structures formed during co-assembly and their relationship to native BMV virions.
To explore potential regulatory pathways for viral RNA packaging in cells.

Main Methods:

Charge detection mass spectrometry (CDMS) was employed to analyze the mass and stoichiometry of assembled particles.
Cryo-electron microscopy (cryo-EM) was utilized to determine the high-resolution structures of the assembled complexes.
In vitro co-assembly experiments were performed using BMV coat proteins and various nucleic acid oligomers.

Main Results:

Co-assembly of BMV coat proteins and nucleic acid oligomers yielded shell structures distinct from native icosahedral virions.
These novel structures were found to be strained and less stable compared to the native BMV virion.
Importantly, these intermediate structures contained significant fragments of native capsid structure, capable of being repurposed.

Conclusions:

The formation of strained, less stable virus-like particles suggests a potential intermediate stage in viral assembly.
These structures provide a reservoir of functional capsid components that can be utilized for forming native virions.
The findings imply a previously unrecognized regulatory mechanism governing selective viral RNA packaging within host cells.