Quantum dot-induced viral capsid assembling in dissociation buffer

Int J Nanomedicine. 2013:8:2119-28. doi: 10.2147/IJN.S44534. Epub 2013 Jun 5.

Abstract

Viruses encapsulating inorganic nanoparticles are a novel type of nanostructure with applications in biomedicine and biosensors. However, the encapsulation and assembly mechanisms of these hybridized virus-based nanoparticles (VNPs) are still unknown. In this article, it was found that quantum dots (QDs) can induce simian virus 40 (SV40) capsid assembly in dissociation buffer, where viral capsids should be disassembled. The analysis of the transmission electron microscope, dynamic light scattering, sucrose density gradient centrifugation, and cryo-electron microscopy single particle reconstruction experimental results showed that the SV40 major capsid protein 1 (VP1) can be assembled into ≈25 nm capsids in the dissociation buffer when QDs are present and that the QDs are encapsulated in the SV40 capsids. Moreover, it was determined that there is a strong affinity between QDs and the SV40 VP1 proteins (KD=2.19E-10 M), which should play an important role in QD encapsulation in the SV40 viral capsids. This study provides a new understanding of the assembly mechanism of SV40 virus-based nanoparticles with QDs, which may help in the design and construction of other similar virus-based nanoparticles.

Keywords: encapsulation; quantum dots; self-assembly; simian virus 40; virus-based nanoparticles.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Buffers
  • Capsid Proteins* / chemistry
  • Capsid Proteins* / metabolism
  • Capsid Proteins* / ultrastructure
  • Capsid* / chemistry
  • Capsid* / metabolism
  • Capsid* / ultrastructure
  • Nanoparticles* / chemistry
  • Nanoparticles* / ultrastructure
  • Particle Size
  • Quantum Dots*
  • Simian virus 40

Substances

  • Buffers
  • Capsid Proteins
  • VP1 protein, polyomavirus