A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids.
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.
Schwartz
Michael
M
Institute for Molecular Virology and Howard Hughes Medical Institute, University of Wisconsin, Madison, Madison, WI 53706, USA.
Chen
Jianbo
J
Janda
Michael
M
Sullivan
Michael
M
den Boon
Johan
J
Ahlquist
Paul
P
D017795:Bromovirus / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D002213:Capsid / Q000235:genetics* / Q000378:metabolism; D046911:Macromolecular Substances; D008954:Models, Biological; D012367:RNA, Viral / Q000235:genetics* / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism; D014779:Virus Replication; D015003:Yeasts / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure
D046911:Macromolecular Substances; D012367:RNA, Viral; D014764:Viral Proteins