ArticleCommunications chemistry2024
From structural polymorphism to structural metamorphosis of the coat protein of flexuous filamentous potato virus Y.
Article in Communications chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Species-specific structural adaptation of the potyviral coat protein in virions and virus-like particles.Communications biology · 2026Article
- Characterization of a multi-segmented rod-shaped mycovirus within the order Martellivirales largely accommodating plant viruses.Virus research · 2025Article
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- High-Fidelity In Vitro Packaging of Diverse Synthetic Cargo into Encapsulin Protein Cages.Angewandte Chemie (International ed. in English) · 2025Article
- Production of Plant Virus-Derived Hybrid Nanoparticles Decorated with Different Nanobodies.ACS nano · 2024Article
- 3D-Printed Self-Assembling Helical Models for Exploring Viral Capsid Structures.Biomimetics (Basel, Switzerland) · 2024Article
- Structural Basis for Alternative Self-Assembly Pathways Leading to Different Human Immunodeficiency Virus Capsid-Like Nanoparticles.ACS nano · 2024Article
- Strategies for controlled assembly of rod-shaped viral particles.Biotechnology advancesReview
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
The structural diversity and tunability of the capsid proteins (CPs) of various icosahedral and rod-shaped viruses have been well studied and exploited in the development of smart hybrid nanoparticles. However, the potential of CPs of the wide-spread flexuous filamentous plant viruses remains to be explored. Here, we show that we can control the shape, size, RNA encapsidation ability, symmetry, stability and surface functionalization of nanoparticles through structure-based design of CP from potato virus Y (PVY). We provide high-resolution insight into CP-based self-assemblies, ranging from large polymorphic or monomorphic filaments to smaller annular, cubic or spherical particles. Furthermore, we show that we can prevent CP self-assembly in bacteria by fusion with a cleavable protein, enabling controlled nanoparticle formation in vitro. Understanding the remarkable structural diversity of PVY CP not only provides possibilities for the production of biodegradable nanoparticles, but may also advance future studies of CP's polymorphism in a biological context.
Identifiers
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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.