From structural polymorphism to structural metamorphosis of the coat protein of flexuous filamentous potato virus Y

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A90127%2F24%3A00139047" target="_blank" >RIV/00216224:90127/24:00139047 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.nature.com/articles/s42004-024-01100-x" target="_blank" >https://www.nature.com/articles/s42004-024-01100-x</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s42004-024-01100-x" target="_blank" >10.1038/s42004-024-01100-x</a>

Jazyk výsledku

angličtina

Název v původním jazyce

From structural polymorphism to structural metamorphosis of the coat protein of flexuous filamentous potato virus Y

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

From structural polymorphism to structural metamorphosis of the coat protein of flexuous filamentous potato virus Y

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10400 - Chemical sciences

Projekt

—

Návaznosti

—

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

COMMUNICATIONS CHEMISTRY

ISSN

2399-3669

e-ISSN

2399-3669

Svazek periodika

7

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

19

Strana od-do

1-19

Kód UT WoS článku

001146671600002

EID výsledku v databázi Scopus

2-s2.0-85182660244