A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids

Mol Cell. 2002 Mar;9(3):505-14. doi: 10.1016/s1097-2765(02)00474-4.

Abstract

We show that brome mosaic virus (BMV) RNA replication protein 1a, 2a polymerase, and a cis-acting replication signal recapitulate the functions of Gag, Pol, and RNA packaging signals in conventional retrovirus and foamy virus cores. Prior to RNA replication, 1a forms spherules budding into the endoplasmic reticulum membrane, sequestering viral positive-strand RNA templates in a nuclease-resistant, detergent-susceptible state. When expressed, 2a polymerase colocalizes in these spherules, which become the sites of viral RNA synthesis and retain negative-strand templates for positive-strand RNA synthesis. These results explain many features of replication by numerous positive strand RNA viruses and reveal that these viruses, reverse transcribing viruses, and dsRNA viruses share fundamental similarities in replication and may have common evolutionary origins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bromovirus / genetics*
  • Bromovirus / metabolism
  • Bromovirus / physiology
  • Capsid / genetics*
  • Capsid / metabolism
  • Macromolecular Substances
  • Models, Biological
  • RNA, Viral / genetics*
  • RNA, Viral / metabolism
  • Viral Proteins / genetics*
  • Viral Proteins / metabolism
  • Virus Replication*
  • Yeasts / genetics
  • Yeasts / metabolism
  • Yeasts / ultrastructure

Substances

  • Macromolecular Substances
  • RNA, Viral
  • Viral Proteins