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Journal of Virology, January 1999, p. 325-333, Vol. 73, No. 1
Section on Microbiology and Virology,
Received 3 August 1998/Accepted 15 October 1998
The sequence of human herpesvirus 6 (HHV-6) U51 open reading frame
predicts a protein of 301 amino acid residues with seven transmembrane
domains. To identify and characterize U51, we derived antipeptide
polyclonal antibodies and developed a transient expression assay. We
ascertained that U51 was synthesized in cord blood mononuclear cells
infected with either variant A- or variant B-HHV-6 and was transported
to the surface of productively infected cells. When synthesized in
transient expression systems, U51 intracellular trafficking was
regulated in a cell-type-dependent fashion. In human monolayer HEK-293
and 143tk
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Trafficking to the Plasma Membrane of the Seven-Transmembrane
Protein Encoded by Human Herpesvirus 6 U51 Gene Involves a
Cell-Specific Function Present in T Lymphocytes
cells, U51 accumulated predominantly in the endoplasmic
reticulum and failed to be transported to the cell surface. In
contrast, in T-lymphocytic cell lines J-Jhan, Molt-3, and Jurkat, U51
was successfully transported to the plasma membrane. We infer that
transport of U51 to the cell surface requires a cell-specific function
present in activated T lymphocytes and T-cell lines.
*
Corresponding author. Mailing address: Dipartimento di
Patologia Sperimentale, Sezione di Microbiologia e Virologia, Via San Giacomo, 12, 40126 Bologna, Italy. Phone: 39 051 354733/34. Fax: 39 051 354747. E-mail: campadel{at}kaiser.alma.unibo.it.
Journal of Virology, January 1999, p. 325-333, Vol. 73, No. 1
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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