# Species-specific structural adaptation of the potyviral coat protein in virions and virus-like particles

## TL;DR

This study explores how the coat protein of potyviruses adapts structurally in virions and virus-like particles, revealing species-specific interactions that influence assembly and stability.

## Contribution

The study identifies species-specific amino acid residues and conserved interactions that govern potyviral virion assembly and stability.

## Key findings

- Potyviral coat proteins have conserved virion structures but species-specific amino acids in CP-CP and CP-RNA interactions.
- Species-specific CP sequences determine the architecture and structural polymorphism of RNA-free virus-like particles.
- A conserved charged amino acid triad is essential for the stability of virions and RNA-free virus-like particles.

## Abstract

Potyviruses are the largest group of plant positive-sense single-stranded RNA viruses and represent a major economic burden worldwide. Their coat protein (CP) forms a filamentous, flexible capsid around the genomic RNA. However, information is still lacking on the mechanisms of virion assembly, disassembly and stability, which is central to understanding virus biology and control. Here, we investigate the role of CP in these processes using structural, biochemical and biophysical studies of five potyviral CPs from three phylogenetic clades combined with bioinformatics and in planta experiments. Our results suggest that, while potyviruses have a conserved virion structure, the amino acids forming the CP-CP and CP-RNA interactions leading to this structure are species-specific. We show that the species-specific CP sequence also determines the architecture of RNA-free virus-like particles (VLPs) and the degree of their structural polymorphism. We identify the residues that determine this specificity at distinct S1-S4 interaction sites. In contrast, a highly conserved charged amino acid triad at the CP-CP interface is essential for the stability of virions and RNA-free VLPs. These results contribute to understanding the molecular mechanism of potyviral virion assembly and highlight the significance of the amino acid sequence of selected CPs in potential biotechnological or biomedical applications.

Structural analysis of potyviruses and virus-like particles reveals the interplay between conserved and species-specific molecular interactions that may guide the formation of structurally uniform virions via species-specific RNA-free intermediates.