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Originally published In Press as doi:10.1074/jbc.M106300200 on August 14, 2001

J. Biol. Chem., Vol. 276, Issue 42, 39226-39231, October 19, 2001
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Characterization of the Signal Peptide Processing and Membrane Association of Human Cytomegalovirus Glycoprotein O*

Regan N. TheilerDagger and Teresa Compton§

From the McArdle Laboratory for Cancer Research, University of Wisconsin-Madison Medical School, Madison, Wisconsin 53706

Human cytomegalovirus (HCMV) has a structurally complex envelope that contains multiple glycoproteins. These glycoproteins are involved in virus entry, virus maturation, and cell-cell spread of infection. Glycoprotein H (gH), glycoprotein L (gL), and glycoprotein O (gO) associate covalently to form a unique disulfide-bonded tripartite complex. Glycoprotein O was recently discovered, and its basic structure, as well as that of the tripartite complex, remains uncharacterized. Based on hydropathy analysis, we hypothesized that gO could adopt a type II transmembrane orientation. The data presented here, however, reveal that the single hydrophobic domain of gO functions as a cleavable signal peptide that is absent from the mature molecule. Although it lacks a membrane anchor, glycoprotein O is associated with the membranes of HCMV-infected cells. The sophisticated organization of the gH·gL·gO complex reflects the intricate nature of the multicomponent entry and fusion machinery encoded by HCMV.

* This research was funded by United States Public Health Service Grant RO1 A144203.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by Molecular Biosciences Training Grant T32 GM 07215.

§ To whom correspondence should be addressed: McArdle Laboratory for Cancer Research, 1400 University Ave., Madison, WI 53706. Tel.: 608-262-1474; Fax: 608-262-2824; E-mail: tcompton@facstaff.wisc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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