Related Experiment Video
Updated: Apr 4, 2026

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
Published on: July 27, 2021
A protein with simultaneous capsid scaffolding and dsRNA-binding activities enhances the birnavirus capsid mechanical
Johann Mertens1,2, Santiago Casado1, Carlos P Mata3
1Instituto Madrileño de Estudios Avanzados en Nanociencia (IMDEA Nanociencia) Campus Cantoblanco, 28049 Madrid, Spain.
Abstract:
Viral capsids are metastable structures that perform many essential processes; they also act as robust cages during the extracellular phase. Viruses can use multifunctional proteins to optimize resources (e.g., VP3 in avian infectious bursal disease virus, IBDV). The IBDV genome is organized as ribonucleoproteins (RNP) of dsRNA with VP3, which also acts as a scaffold during capsid assembly. We characterized mechanical properties of IBDV populations with different RNP content (ranging from none to four RNP). The IBDV population with the greatest RNP number (and best fitness) showed greatest capsid rigidity. When bound to dsRNA, VP3 reinforces virus stiffness. These contacts involve interactions with capsid structural subunits that differ from the initial interactions during capsid assembly. Our results suggest that RNP dimers are the basic stabilization units of the virion, provide better understanding of multifunctional proteins, and highlight the duality of RNP as capsid-stabilizing and genetic information platforms.
Related Concept Videos
Viral Structure
Single-Strand DNA Binding Proteins
Size and Structure of Viral Genomes
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Viruses with RNA Genomes
Introduction to Virus

