Double-membraned liposomes sculpted by poliovirus 3AB protein

J Biol Chem. 2013 Sep 20;288(38):27287-27298. doi: 10.1074/jbc.M113.498899. Epub 2013 Aug 1.

Abstract

Infection with many positive-strand RNA viruses dramatically remodels cellular membranes, resulting in the accumulation of double-membraned vesicles that resemble cellular autophagosomes. In this study, a single protein encoded by poliovirus, 3AB, is shown to be sufficient to induce the formation of double-membraned liposomes via the invagination of single-membraned liposomes. Poliovirus 3AB is a 109-amino acid protein with a natively unstructured N-terminal domain. HeLa cells transduced with 3AB protein displayed intracellular membrane disruption; specifically, the formation of cytoplasmic invaginations. The ability of a single viral protein to produce structures of similar topology to cellular autophagosomes should facilitate the understanding of both cellular and viral mechanisms for membrane remodeling.

Keywords: Lipoprotein; Liposomes; Membrane Bilayer; Membrane Biophysics; Membrane Reconstitution; Positive-strand RNA Viruses; Viral Protein; Viral Replication.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Membrane / chemistry*
  • Cell Membrane / genetics
  • Cell Membrane / metabolism
  • HeLa Cells
  • Humans
  • Liposomes / chemistry*
  • Liposomes / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Poliovirus*
  • Protein Structure, Tertiary
  • Viral Nonstructural Proteins / chemistry*
  • Viral Nonstructural Proteins / genetics
  • Viral Nonstructural Proteins / metabolism

Substances

  • 3AB protein, poliovirus
  • Liposomes
  • Membrane Proteins
  • Viral Nonstructural Proteins