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Departments of
*
Immunobiology and
Oral Medicine and Pathology, Guy’s, King’s & St. Thomas’ Hospital Medical Schools, London, United Kingdom
The C-C chemokine receptor CCR5 serves an important function in
chemotaxis of lymphocytes, monocytes, and dendritic cells. CCR5 is also
the major coreceptor in most macrophage-tropic HIV-1 infections.
Immunization of rhesus macaques with a baculovirus-generated CCR5
construct or peptides derived from the sequences of the four
extracellular domains of CCR5 elicited IgG and IgA Abs, inhibition of
SIV replication, and CD4+ T cell proliferative responses to
three of the extracellular domains of CCR5. The immune sera reacted
with cell surface CCR5 expressed on HEK 293 cells. T and B cell epitope
mapping revealed major and minor T and B cell epitopes in the
N-terminal, first, and second loops of CCR5. The three C-C chemokines,
RANTES, macrophage-inflammatory protein-1
, and
macrophage-inflammatory protein-1
, were up-regulated by immunization
with the CCR5-derived peptides, and the cell surface expression of CCR5
was decreased. The CCR5 Abs were complementary to the C-C chemokines in
inhibiting HIV replication in vitro. Immunization with the four
extracellular domains of CCR5 suggests that three of them are
immunogenic, with maximal T cell responses being elicited by the second
loop peptide. However, maximal Abs to the cell surface CCR5 or viral
inhibitory Abs in vitro were induced by the N-terminal peptide.
Up-regulation of the three C-C chemokines and down-modulation of cell
surface CCR5 were elicited by the second loop, N-terminal, and first
loop peptides. The data suggest that a dual mechanism of C-C chemokines
and specific Abs may engage and down-modulate the CCR5 coreceptors and
prevent in vitro HIV or SIV replication.
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