Self-Assembly of Viral Capsid Proteins Driven by Compressible Nanobubbles

J Phys Chem Lett. 2020 Dec 17;11(24):10421-10424. doi: 10.1021/acs.jpclett.0c02658. Epub 2020 Dec 3.

Abstract

Colloidal nanobubbles occur in gas-saturated aqueous solutions following high power water electrolysis. Here the influence of nanobubble solutions on the self-assembly properties of viral capsid proteins (CP) was investigated. Interestingly, we found that gas solutions were able to trigger the self-assembly of CP of cowpea chlorotic mottle virus (CCMV) in the absence of the viral genome, most likely by acting as a negatively charged template. The process was demonstrated by three distinct techniques, namely, dynamic light scattering (DLS), atomic force microscopy (AFM), and transmission electron microscopy (TEM). Furthermore, nanobubble-induced self-assembly of viral CP was found to depend on protein concentration. Low CP concentrations led to assembly of 18 nm virus-like particles (VLPs), comparable to T = 1 (Casper and Klug triangulation number) virus capsids, whereas high CP concentrations led to 28 nm VLPs (similar to T = 3 capsids). This paves a new route for self-assembly of VLPs.

MeSH terms

  • Bromovirus / chemistry*
  • Capsid Proteins / chemistry*
  • Dynamic Light Scattering
  • Microscopy, Atomic Force
  • Microscopy, Electron, Transmission
  • Nanostructures / chemistry*

Substances

  • Capsid Proteins