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Vol. 12, Issue 6, 1737-1749, June 2001
and
*Medical Research Council Laboratory for Molecular Cell Biology and
Department of Biochemistry, University College London, London WC1E 6BT,
United Kingdom; and Genes encoding chemokine receptor-like proteins have been found in
herpes and poxviruses and implicated in viral pathogenesis. Here we
describe the cellular distribution and trafficking of a human
cytomegalovirus (HCMV) chemokine receptor encoded by the US28 gene, after transient and stable expression in
transfected HeLa and Cos cells. Immunofluorescence staining indicated
that this viral protein accumulated intracellularly in vesicular
structures in the perinuclear region of the cell and showed overlap
with markers for endocytic organelles. By immunogold electron
microscopy US28 was seen mostly to localize to multivesicular
endosomes. A minor portion of the protein (at most 20%) was also
expressed at the cell surface. Antibody-feeding experiments indicated
that cell surface US28 undergoes constitutive ligand-independent
endocytosis. Biochemical analysis with the use of iodinated ligands
showed that US28 was rapidly internalized. The high-affinity ligand of US28, the CX3C-chemokine fractalkine, reduced the
steady-state levels of US28 at the cell surface, apparently by
inhibiting the recycling of internalized receptor. Endocytosis and
cycling of HCMV US28 could play a role in the sequestration of host
chemokines, thereby modulating antiviral immune responses. In addition,
the distribution of US28 mainly on endosomal membranes may allow it to
be incorporated into the viral envelope during HCMV assembly.
Laboratory for Molecular
Pharmacology, The Panum Institute, University of Copenhagen, DK-2200
Copenhagen, Denmark
Present address: Department of
Microbiology and Immunology, Stanford University School of Medicine,
Stanford, CA 94305-5124.
§
Corresponding author. E-mail address:
m.marsh{at}ucl.ac.uk.
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