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Picower Institute for Medical Research, Manhasset, NY 11030
It is now well established that HIV-1 requires interactions with
both CD4 and a chemokine receptor on the host cell surface for
efficient infection. The expression of the CCR5 chemokine receptor in
human macrophages facilitates HIV-1 entry into these cells, which are
considered important in HIV pathogenesis not only as viral reservoirs
but also as modulators of altered inflammatory function in HIV disease
and AIDS. LPS, a principal constituent of Gram-negative bacterial cell
walls, is a potent stimulator of macrophages and has been shown to
inhibit HIV infection in this population. We now present evidence that
one mechanism by which LPS mediates its inhibitory effect on HIV-1
infection is through a direct and unusually sustained down-regulation
of cell-surface CCR5 expression. This LPS-mediated down-regulation of
CCR5 expression was independent of de novo protein synthesis and
differed from the rapid turnover of these chemokine receptors observed
in response to two natural ligands, macrophage-inflammatory
protein-1
and -1ß. LPS did not act by down-regulating CCR5 mRNA
(mRNA levels actually increased slightly after LPS treatment) or by
enhancing the degradation of internalized receptor. Rather, the
observed failure of LPS-treated macrophages to rapidly restore CCR5
expression at the cell-surface appeared to result from altered
recycling of chemokine receptors. Taken together, our results suggest a
novel pathway of CCR5 recycling in LPS-stimulated human macrophages
that might be targeted to control HIV-1
infection.
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