Abstract
Plant viruses and their virus-like particles (VLPs) have a lot of advantages for biotechnological applications including complete safety for humans. Alternanthera mosaic virus (AltMV) is a potentially promising object for design of novel materials. The 3D structures of AltMV virions and its VLPs were obtained by single particle EM at ~13Å resolution. The comparison of the reconstructions and a trypsin treatment revealed that AltMV CPs possesses a different fold in the presence (virions) and absence of viral RNA (VLPs). For the first time, the structure of morphologically similar virions and virus-like particles based on the coat protein of a helical filamentous plant virus is shown to be different. Despite this, both AltMV virions and VLPs are stable in a wide range of conditions. To provide a large amount of AltMV for biotechnology usage the isolation procedure was modified.
MeSH terms
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Capsid Proteins / chemistry*
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Microscopy, Electron / methods
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Mosaic Viruses / chemistry*
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Virion / chemistry*
Grants and funding
This work (study design, data collection and analysis) was funded by the Russian Science Foundation (Grant No. 14-24-00007) to JGA.
www.rscf.ru. Building the 3D reconstructions was funded by Russian Foundation for Basic Research (Grant No. 16-34-00658_mol_a to EP).
www.rfbr.ru. Currently one of the authors (Pechnikova E.V.) is employed by a commercial company ‘Thermo Fisher Scientific’. The presented cryo-EM results were obtained in V.A. Shoubnikov Institute of Crystallography RAS and National Research Centre ‘Kurchatov Institute’, where Pechnikova E.V. was employed at that time. ‘Thermo Fisher Scientific’ provided support in the form of salary for author [Pechnikova E.V.], but did not have any additional role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. The specific role of this author is articulated in the ‘author contributions’ section.