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N36, a synthetic N-terminal heptad repeat domain of the HIV-1 envelope protein gp41, is an activator of human phagocytes

  1. Author:
    Le, Y. Y.
    Jiang, S.
    Hu, J. Y.
    Gong, W. H.
    Su, S. B.
    Dunlop, N. M.
    Shen, W. P.
    Li, B. Q.
    Wang, J. M.

  2. Author Address

    NCI, Frederick Canc Res & Dev Ctr, Mol Immunoregulat Lab, Div Basic Sci, Bldg 560, Room 31-40, Ft Detrick, MD 21702 USA. NCI, Frederick Canc Res & Dev Ctr, Mol Immunoregulat Lab, Div Basic Sci, Ft Detrick, MD 21702 USA. NCI, Frederick Canc Res & Dev Ctr, SAIC Frederick, Intramural Res Support Program, Ft Detrick, MD 21702 USA. New York Blood Ctr, Lindsley F Kimball Res Inst, New York, NY 10021 USA.
    1. Year: 2000
  2. Journal: Clinical Immunology
    1. 96
    2. 3
    3. Pages: 236-242
  4. Type of Article: Article
  1. Abstract:

    Human immunodeficiency virus type 1 (HIV-1) envelope protein gp41 mediates viral fusion with human host cells. In this study we show that N36, a synthetic peptide derived from the N- terminus of gp41, induced directional migration and calcium mobilization in human monocytes and neutrophils, The activity of N36 on phagocytes was pertussis toxin sensitive, suggesting involvement of a Gi-coupled seven-transmembrane receptor(s), Since high concentrations of the bacterial chemotactic peptide fMet-Leu-Phe (fMLF) partially desensitized the calcium mobilizing activity of N36 in phagocytes, we postulated that N36 might use a low-affinity fMLF receptor. By using cells stably expressing fMLF receptor FPR or FPRL1, we demonstrate that N36 uses FPRL1 as a functional receptor. Our results suggest that HIV-1 gp41 may contain a fragment(s) that activates the innate host immune cells through FPRL1, Since the activation of FPRL1 in monocytes has been shown to heterologously desensitize chemokine receptors, the reduced phagocyte response to chemoattractants seen in AIDS patients may be attributed, at least in part, to heterologous desensitization. (C) 2000 Academic Press.

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