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Journal of Virology, November 1999, p. 9515-9520, Vol. 73, No. 11
Division of Virology, Department of
Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom
Received 3 June 1999/Accepted 28 July 1999
Glycoprotein D (gD) of herpes simplex virus type 1 (HSV-1) was
modified to encode targeting signals known to localize proteins to
either the endoplasmic reticulum (ER) or the trans-Golgi
network. These motifs conferred the predicted targeting properties on
gD in transfected cells as judged by immunofluorescence staining, and
the exclusion of targeted gD from the cell surface was confirmed by the
fact that these molecules exhibited substantially reduced activity in
cell-cell fusion assays. Recombinant viruses expressing Golgi-targeted
forms of gD grew to wild-type levels in noncomplementing cells,
exhibited unaltered particle/infectivity ratios, and were found to
contain wild-type levels of gD, whereas a recombinant expressing
ER-retained gD was helper cell dependent and, when grown on
noncomplementing cells, produced virions of low specific infectivity
with greatly reduced levels of gD. These data imply that HSV-1 acquires
its final membrane from a post-ER compartment and lend support to the
view that the virus undergoes de-envelopment and reenvelopment steps
during virus egress.
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Effects of Targeting Herpes Simplex Virus Type 1 gD
to the Endoplasmic Reticulum and trans-Golgi
Network
*
Corresponding author. Mailing address: Division of
Virology, Department of Pathology, University of Cambridge, Tennis
Court Rd., Cambridge CB2 1QP, United Kingdom. Phone: 01223 336920. Fax: 01223 336926. E-mail: acm{at}mole.bio.cam.ac.uk.
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