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CUTTING EDGE |
*
Division of Molecular Immunology, La Jolla Institute for Allergy and Immunology, San Diego, CA 92121;
Department of Immunology and Microbiology, Rush Medical College, Chicago, IL 60612;
Department of Medicine, University of California at San Diego, La Jolla CA 92093; and
§
Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland
The UL144 open reading frame found in clinical isolates of human CMV (HCMV) encodes a structural homologue of the herpesvirus entry mediator, a member of the TNFR superfamily. UL144 is a type I transmembrane glycoprotein that is expressed early after infection of fibroblasts; however, it is retained intracellularly. A YXXZ motif in the highly conserved cytoplasmic tail contributes to UL144 subcellular distribution. The finding that no known ligand of the TNF family binds UL144 suggests that its mechanism of action is distinct from other known viral immune evasion genes. Specific Abs to UL144 can be detected in the serum of a subset of HCMV seropositive individuals infected with HIV. This work establishes a novel molecular link between the TNF superfamily and herpesvirus that may contribute to the ability of HCMV to escape immune clearance.
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