Structure and properties of virions and virus-like particles derived from the coat protein of Alternanthera mosaic virus.
basic_science · Level V
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- Record sourced from PubMed, PMID 28837650.
- Also identified by DOI 10.1371/journal.pone.0183824 and PMC identifier 5570366.
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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.
Medical subject headings
- Capsid Proteins
- Mosaic Viruses
- Virion