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Blood, Vol. 94 No. 4 (August 15), 1999:
pp. 1165-1173
A Synthetic Peptide Derived From Human Immunodeficiency Virus Type 1 gp120 Downregulates the Expression and Function of Chemokine Receptors
CCR5 and CXCR4 in Monocytes by Activating the 7-Transmembrane
G-Protein-Coupled Receptor FPRL1/LXA4R
Xiyun Deng,
Hirotsugu Ueda,
Shao Bo Su,
Wanghua Gong,
Nancy M. Dunlop,
Ji-Liang Gao,
Philip M. Murphy, and
Ji Ming Wang
From the Laboratory of Molecular Immunoregulation, Division of Basic
Sciences, and the Intramural Research Support Program, SAIC Frederick,
National Cancer Institute-Frederick Cancer Research and Development
Center, Frederick, MD; and the Laboratory of Host Defenses, National
Institute of Allergy and Infectious Diseases, National Institutes of
Health, Bethesda, MD.
Because envelope gp120 of various strains of human immunodeficiency
virus type 1 (HIV-1) downregulates the expression and function of a variety of chemoattractant receptors through a process of
heterologous desensitization, we investigated whether epitopes derived
from gp120 could mimic the effect. A synthetic peptide domain,
designated F peptide, corresponding to amino acid residues 414-434 in
the V4-C4 region of gp120 of the HIV-1 Bru strain, potently reduced
monocyte binding and chemotaxis response to macrophage inflammatory
protein 1 (MIP-1) and stromal cell-derived factor 1
(SDF-1), chemokines that use the receptors CCR5 and
CXCR4, respectively. Further study showed that F peptide by itself is an inducer of chemotaxis and calcium mobilization in human monocytes and neutrophils. In cross-desensitization experiments, among the numerous chemoattractants tested, only the bacterial chemotactic peptide fMLF, when used at high concentrations, partially attenuated calcium mobilization induced by F peptide in phagocytes, suggesting that this peptide domain might share a 7-transmembrane,
G-protein-coupled receptor with fMLF. By using cells transfected with
cDNAs encoding receptors that interact with fMLF, we found that F
peptide uses an fMLF receptor variant, FPRL1, as a functional receptor.
The activation of monocytes by F peptide resulted in downregulation of
the cell surface expression of CCR5 and CXCR4 in a protein kinase
C-dependent manner. These results demonstrate that activation of FPRL1
on human moncytes by a peptide domain derived from HIV-1 gp120 could
lead to desensitization of cell response to other chemoattractants.
This may explain, at least in part, the initial activation of innate
immune responses in HIV-1-infected patients followed by immune suppression.
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