Controlling Viral Capsid Assembly with Templating

TL;DR

This paper presents coarse-grained models for viral capsid assembly around nanoparticles, revealing cooperative interactions that enhance assembly efficiency and differ from empty capsid formation, with implications for virology and nanomaterials.

Contribution

The study introduces novel models describing nanoparticle-assisted capsid assembly, highlighting unique cooperative pathways not seen in spontaneous empty capsid formation.

Findings

Cooperative interactions significantly improve assembly rates.

Large core-subunit interactions lead to disordered adsorption and cooperative rearrangement.

Models align with recent experimental observations.

Abstract

We develop coarse-grained models that describe the dynamic encapsidation of functionalized nanoparticles by viral capsid proteins. We find that some forms of cooperative interactions between protein subunits and nanoparticles can dramatically enhance rates and robustness of assembly, as compared to the spontaneous assembly of subunits into empty capsids. For large core-subunit interactions, subunits adsorb onto core surfaces en masse in a disordered manner, and then undergo a cooperative rearrangement into an ordered capsid structure. These assembly pathways are unlike any identified for empty capsid formation. Our models can be directly applied to recent experiments in which viral capsid proteins assemble around the functionalized inorganic nanoparticles [Sun et al., Proc. Natl. Acad. Sci (2007) 104, 1354]. In addition, we discuss broader implications for understanding the dynamic encapsidation of single-stranded genomic molecules during viral replication and for developing multicomponent nanostructured materials.