ArticlePloS one2017
Structure and properties of virions and virus-like particles derived from the coat protein of Alternanthera mosaic virus.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- From structural polymorphism to structural metamorphosis of the coat protein of flexuous filamentous potato virus Y.Communications chemistry · 2024Article
- CryoEM and stability analysis of virus-like particles of potyvirus and ipomovirus infecting a common host.Communications biology · 2023Article
- Rapid, Sensitive and Simultaneous Detection of Two Wheat RNA Viruses Using Reverse Transcription Recombinase Polymerase Amplification (RT-RPA).Life (Basel, Switzerland) · 2022Article
- Thermal remodelling of Alternanthera mosaic virus virions and virus-like particles into protein spherical particles.PloS one · 2021Article
- Turnip Mosaic Virus Coat Protein Deletion Mutants Allow Defining Dispensable Protein Domains for 'in Planta' eVLP Formation.Viruses · 2020Article
- A Recombinant Rotavirus Antigen Based on the Coat Protein of Alternanthera Mosaic Virus.Molecular biology · 2020Article
- Structure of Turnip mosaic virus and its viral-like particles.Scientific reports · 2019Article
- Structural basis for the multitasking nature of the potato virus Y coat protein.Science advances · 2019Article
- Thermally-responsive Virus-like Particle for Targeted Delivery of Cancer Drug.Scientific reports · 2019Article
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Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.