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Journal of Virology, December 2001, p. 12209-12219, Vol. 75, No. 24
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.24.12209-12219.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Intracellular Trafficking of the UL11 Tegument
Protein of Herpes Simplex Virus Type 1
Joshua S.
Loomis,
J. Bradford
Bowzard,
Richard J.
Courtney, and
John W.
Wills*
Department of Microbiology and Immunology,
The Pennsylvania State University College of Medicine, Hershey,
Pennsylvania 17033
Received 19 July 2001/Accepted 10 September 2001
Growing evidence indicates that herpes simplex virus type 1 (HSV-1)
acquires its final envelope in the trans-Golgi network (TGN). During
the envelopment process, the viral nucleocapsid as well as the envelope
and tegument proteins must arrive at this site in order to be
incorporated into assembling virions. To gain a better understanding of
how these proteins associate with cellular membranes and target to the
correct compartment, we have been studying the intracellular
trafficking properties of the small tegument protein encoded by the
UL11 gene of HSV-1. This 96-amino-acid, myristylated
protein accumulates on the cytoplasmic face of internal membranes,
where it is thought to play a role in nucleocapsid envelopment and
egress. When expressed in the absence of other HSV-1 proteins, the UL11
protein localizes to the Golgi apparatus, and previous deletion
analyses have revealed that the membrane-trafficking information is
contained within the first 49 amino acids. The goal of this study was
to map the functional domains required for proper Golgi membrane
localization. In addition to N-terminal myristylation, which allows for
weak membrane binding, UL11 appears to be palmitylated on one or more
of three consecutive N-terminal cysteines. Using membrane-pelleting
experiments and confocal microscopy, we show that palmitylation of UL11
is required for both Golgi targeting specificity and strong membrane
binding. Furthermore, we found that a conserved acidic cluster within
the first half of UL11 is required for the recycling of this tegument
protein from the plasma membrane to the Golgi apparatus. Taken
together, our results demonstrate that UL11 has highly dynamic
membrane-trafficking properties, which suggests that it may play
multiple roles on the plasma membrane as well as on the nuclear and TGN membranes.
*
Corresponding author. Mailing address: Department of
Microbiology and Immunology, The Pennsylvania State University College of Medicine, 500 University Dr., P.O. Box 850, Hershey, PA 17033. Phone: (717) 531-3528. Fax: (717) 531-6522. E-mail:
jwills{at}psu.edu.

Present address: Department of Biochemistry, Emory University
School of Medicine, Atlanta, GA
30322.
Journal of Virology, December 2001, p. 12209-12219, Vol. 75, No. 24
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.24.12209-12219.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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