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J Virol, July 1998, p. 5717-5727, Vol. 72, No. 7
Department of Stomatology, School of
Dentistry, University of California San Francisco, San Francisco,
California 94143-0512,1 and
Department
of Molecular Biology, Wyeth-Ayerst Research, Pearl River, New York
109652
Received 13 January 1998/Accepted 17 March 1998
Processes by which human herpesviruses penetrate and are released
from polarized epithelial cells, which have distinct apical and
basolateral membrane domains differing in protein and lipid content,
are poorly understood. We recently reported that human cytomegalovirus (CMV) mutants with deletions of the gene US9 formed wild-type plaques in cultures of human fibroblasts but were impaired in
the capacity for cell-to-cell spread in polarized human retinal pigment
epithelial cells. Unlike the glycoproteins that are required for
infection, the protein encoded by CMV US9 plays an accessory role by
promoting dissemination of virus across cell-cell junctions of
polarized epithelial cells. To identify the product and investigate its
specialized functions, we selected Madine-Darby canine kidney II (MDCK)
epithelial cells that constitutively express CMV US9 or, as a control,
US8. The gene products, designated gpUS9 and gpUS8, were glycosylated
proteins of comparable molecular masses but differed considerably in
intracellular distribution and solubility. Immunofluorescence laser
scanning confocal microscopy indicated that, like gpUS8, gpUS9 was
present in the endoplasmic reticulum and Golgi compartments of
nonpolarized cells. In polarized epithelial cells, gpUS9 also
accumulated along lateral membranes, colocalizing with cadherin and
actin, and was insoluble in Triton X-100, a property shared with
proteins that associate with the cytoskeleton. We hypothesize that
gpUS9 may enhance the dissemination of CMV in infected epithelial
tissues by associating with the cytoskeletal matrix.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
A Novel Human Cytomegalovirus Glycoprotein, gpUS9, Which Promotes
Cell-to-Cell Spread in Polarized Epithelial Cells, Colocalizes with
the Cytoskeletal Proteins E-Cadherin and F-Actin
*
Corresponding author. Mailing address: Department of
Stomatology, School of Dentistry, University of California San
Francisco, 513 Parnassus Ave., San Francisco, CA 94143-0512. Phone:
(415) 476-8248. Fax: (415) 502-7338. E-mail:
pereira{at}itsa.ucsf.edu.
J Virol, July 1998, p. 5717-5727, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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