Recombinant VP4 of human rhinovirus induces permeability in model membranes

Matthew P Davis1, Graham Bottley, Lucy P Beales

  • 1Institute for Molecular and Cellular Biology, Faculty of Biological Sciences, The University of Leeds, Leeds LS2 9JT, United Kingdom.

Journal of Virology
|February 8, 2008
PubMed

Insights

Picornavirus entry into cells is unclear. Researchers found that the VP4 protein from human rhinovirus 16 can disrupt liposome membranes, suggesting VP4 is key to viral cell entry.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Picornaviruses are nonenveloped viruses.
  • The mechanism of picornavirus membrane penetration during cell entry is not well understood.
  • The capsid protein VP4 has been implicated in picornavirus cell entry.

Purpose of the Study:

  • To investigate the role of picornavirus VP4 protein in membrane penetration.
  • To provide evidence for VP4's function in viral cell entry.

Main Methods:

  • Produced recombinant VP4 protein from human rhinovirus 16.
  • Assayed the ability of VP4 to associate with and induce permeability in liposomes.

Main Results:

  • Recombinant VP4 associated with liposomes.
  • VP4 induced membrane permeability in intact liposomes.

Conclusions:

  • VP4 plays a significant role in picornavirus membrane penetration.
  • These findings support the hypothesis that VP4 is essential for picornavirus cell entry.