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Vol. 12, Issue 7, 2031-2046, July 2001
European Molecular Biology Laboratory, Cell Biology and
Biophysics Programme, 69117 Heidelberg, Germany
Vaccinia virus (vv), a member of the poxvirus family, is unique
among most DNA viruses in that its replication occurs in the cytoplasm
of the infected host cell. Although this viral process is known to
occur in distinct cytoplasmic sites, little is known about its
organization and in particular its relation with cellular membranes.
The present study shows by electron microscopy (EM) that soon after
initial vv DNA synthesis at 2 h postinfection, the sites become
entirely surrounded by membranes of the endoplasmic reticulum (ER).
Complete wrapping requires ~45 min and persists until virion assembly
is initiated at 6 h postinfection, and the ER dissociates from the
replication sites. [3H]Thymidine incorporation at
different infection times shows that efficient vv DNA synthesis
coincides with complete ER wrapping, suggesting that the ER facilitates
viral replication. Proteins known to be associated with the nuclear
envelope in interphase cells are not targeted to these
DNA-surrounding ER membranes, ruling out a role for these molecules in
the wrapping process. By random green fluorescent protein-tagging of vv
early genes of unknown function with a putative transmembrane domain, a
novel vv protein, the gene product of E8R, was identified that is
targeted to the ER around the DNA sites. Antibodies raised against this vv early membrane protein showed, by immunofluorescence microscopy, a
characteristic ring-like pattern around the replication site. By
electron microscopy quantitation the protein concentrated in the ER
surrounding the DNA site and was preferentially targeted to membrane
facing the inside of this site. These combined data are discussed in
relation to nuclear envelope assembly/disassembly as it occurs during
the cell cycle.
Corresponding author. E-mail address:
krijnse{at}embl-heidelberg.de.
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