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Blood, Vol. 93 No. 11 (June 1), 1999:
pp. 3885-3892
T20/DP178, an Ectodomain Peptide of Human Immunodeficiency Virus Type 1 gp41, Is an Activator of Human Phagocyte N-Formyl Peptide Receptor
Shao Bo Su,
Wang-hua Gong,
Ji-Liang Gao,
Wei-Ping Shen,
Michael C. Grimm,
Xiyun Deng,
Philip M. Murphy,
Joost J. Oppenheim, and
Ji
Ming Wang
From the Laboratory of Molecular Immunoregulation, Division of Basic
Sciences, and 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.
Human immunodeficiency virus type 1 (HIV-1) envelope protein gp41
mediates viral fusion with human host cells. The peptide segment
T20/DP178, located in the C-terminus of the ectodomain of gp41,
interacts with the N-terminal leucine zipper-like domain on gp41 to
establish the fusogenic conformation of the virus. Synthetic T20/DP178
peptide is highly efficacious in inhibiting HIV-1 infection in vitro by
disrupting the transformation of fusogenic status of viral gp41; thus,
it has been proposed for clinical trial. We report that synthetic
T20/DP178 is a chemoattractant and activator of human peripheral blood
phagocytes but not of T lymphocytes. We further demonstrate that
T20/DP178 specifically activates a seven-transmembrane,
G-protein-coupled phagocyte receptor for N-formylated chemotactic
peptides, formyl peptide receptor (FPR). Moreover,
synthetic T20/DP178 analogs lacking N-terminal amino acids acted as FPR
antagonists. Our results suggest that gp41 peptides regulate phagocyte
function via FPR and identify a novel mechanism by which HIV-1 may
modulate innate immunity.
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