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National Institute on Aging, National Institutes of Health, Gerontology Research Center, Baltimore, MD 21224
HIV requires cholesterol and lipid rafts on target cell membranes
for infection. To elucidate a possible mechanism, we determined that
cholesterol extraction by hydroxypropyl-
-cyclodextrin (BCD)
inhibits stromal cell-derived factor 1
(SDF-1) binding to CXCR4
on T cell lines and PBMCs. Intracellular calcium responses to SDF-1,
as well as receptor internalization, were impaired in treated T cells.
Loss in ligand binding is likely due to conformational changes in CXCR4
and not increased sensitivity to internalization. SDF-1 binding and
calcium responses were effectively restored by reloading cholesterol.
Immunofluorescence microscopy revealed that SDF-1 binding occurred
in lipid raft microdomains that contained GM1. CXCR4 surface
expression, on the other hand, only partially colocalized with GM1.
HIV-1IIIB infection assays confirmed the functional loss of
CXCR4 in the cell lines tested, Sup-T1 and CEM-NKR-CCR5. These data
suggest that cholesterol is essential for CXCR4 conformation and
function and that lipid rafts may play a regulatory role in SDF-1
signaling.
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