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Journal of Virology, November 1998, p. 8933-8942, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
The Herpes Simplex Virus gE-gI Complex Facilitates
Cell-to-Cell Spread and Binds to Components of Cell Junctions
Kevin S.
Dingwell1,2 and
David C.
Johnson2,*
Department of Biology, McMaster University,
Hamilton, Ontario, Canada L8N 3Z5,1 and
Department of Molecular Immunology, and Microbiology,
Oregon Health Sciences University, Portland, Oregon
972012
Received 22 June 1998/Accepted 5 August 1998
The herpes simplex virus (HSV) glycoprotein complex gE-gI mediates
the spread of viruses between adjacent cells, and this property is
especially evident for cells that form extensive cell junctions, e.g.,
epithelial cells, fibroblasts, and neurons. Mutants lacking gE or gI
are not compromised in their ability to enter cells as extracellular
viruses. Therefore, gE-gI functions specifically in the movement of
virus across cell-cell contacts and, as such, provides a molecular
handle on this poorly understood process. We expressed gE-gI in human
epithelial cells by using replication-defective adenovirus (Ad)
vectors. gE-gI accumulated at lateral surfaces of the epithelial cells,
colocalizing with the adherens junction protein
-catenin but was not
found on either the apical or basal plasma membranes and did not
colocalize with ZO-1, a component of tight junctions. In subconfluent
monolayers, gE-gI was found at cell junctions but was absent from those
lateral surfaces not in contact with another cell, as was the case for
-catenin. Similar localization of gE-gI to cell junctions was
observed in HSV-infected epithelial cells. By contrast, HSV
glycoprotein gD, expressed using a recombinant Ad vectors, was found
primarily along the apical surfaces of cells, with little or no protein
found on the basal or lateral surfaces. Expression of gE-gI without
other HSV polypeptides did not cause redistribution of either ZO-1 or
-catenin or alter tight-junction functions. Together these results
support a model in which gE-gI accumulates at sites of cell-cell
contact by interacting with junctional components. We hypothesize that gE-gI mediates transfer of HSV across cell junctions by virtue of these
interactions with cell junction components.
*
Corresponding author. Mailing address: L-220 Dept. of
Molecular Microbiology and Immunology, Oregon Health Sciences
University, 3181 S.W. Sam Jackson Park Rd., L220, Portland, OR 97201. Phone: (503) 494-0834. Fax: (503) 494-6862. E-mail:
johnsoda{at}ohsu.edu.
Journal of Virology, November 1998, p. 8933-8942, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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