Self-assembly of sapovirus recombinant virus-like particles from polyprotein in mammalian cells

Microbiol Immunol. 2009 Jan;53(1):49-52. doi: 10.1111/j.1348-0421.2008.00086.x.

Abstract

The SaV genome is a positive-sense, non-segmented single-strand RNA molecule of approximately 7.5 kb that is polyadenylated at its 3' terminus. The major capsid (VP1) of SaV is thought to be produced as the ORF1 polyprotein followed by cleavage, or translation from subgenomic RNA (3'-coterminal with the virus genome), or both. We have recently reported the formation of SaV VLP from subgenomic-like RNA in mammalian cells. In the present study, we demonstrated that the VP1 cleaved from a part of ORF1 polyprotein self-assembled into VLP in mammalian cells when a transient expression system using a recombinant vaccinia virus encoding T7 RNA polymerase was used.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • COS Cells
  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism*
  • Chlorocebus aethiops
  • Polyproteins / genetics
  • Polyproteins / metabolism*
  • Sapovirus / genetics
  • Sapovirus / physiology*
  • Virion / genetics
  • Virion / physiology*
  • Virus Assembly*

Substances

  • Capsid Proteins
  • Polyproteins