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J Biol Chem, Vol. 273, Issue 22, 13430-13436, May 29, 1998
Intracellular Transport of the Glycoproteins gE and gI of the
Varicella-Zoster Virus
gE ACCELERATES THE MATURATION OF gI AND DETERMINES ITS
ACCUMULATION IN THE TRANS-GOLGI NETWORK
Agustín
Alconada,
Ulrike
Bauer,
Laurence
Baudoux§,
Jacques
Piette§, and
Bernard
Hoflack
From the Institut de Biologie de Lille (IFR3), Institut Pasteur de
Lille, 59021 Lille, France and § Laboratory of Fundamental
Virology, Institute of Pathology, University of Liège, B-4000
Liège, Belgium
The varicella-zoster virus (VZV) is the
etiological agent of two different human pathologies, chickenpox
(varicella) and shingles (zoster). This alphaherpesvirus is believed to
acquire its lipidic envelope in the trans-Golgi network (TGN). This is
consistent with previous data showing that the most abundant VZV
envelope glycoprotein gE accumulates at steady-state in this organelle when expressed from cloned cDNA. In the present study, we have investigated the intracellular trafficking of gI, another VZV envelope
glycoprotein. In transfected cells, this protein shows a very slow
biosynthetic transport to the cell surface where it accumulates.
However, upon co-expression of gE, gI experiences a dramatic increase
in its exit rate from the endoplasmic reticulum, it accumulates in a
sialyltransferase-positive compartment, presumably the TGN, and cycles
between this compartment and the cell surface. This differential
behavior results from the ability of gE and gI to form a complex in the
early stages of the biosynthetic pathway whose intracellular traffic is
exclusively determined by the sorting information in the tail of gE.
Thus, gI provides the first example of a molecule localized to the TGN
by means of its association with another TGN protein. We also show
that, during the early stages of VZV infection, both proteins are also
found in the TGN of the host cell. This suggests the existence of an
intermediate stage during VZV biogenesis in which the envelope
glycoproteins, transiently arrested in the TGN, could promote the
envelopment of newly synthesized nucleocapsids into this compartment
and, therefore, the assembly of infective viruses.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
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