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Functional expression of CD4, CXCR4, and CCR5 in glycosphingolipid-deficient mouse melanoma GM95 cells and susceptibility to HIV-1 envelope glycoprotein-triggered membrane fusion

  1. Author:
    Rawat, S. S.
    Eaton, J.
    Gallo, S. A.
    Martin, T. D.
    Ablan, S.
    Ratnayake, S.
    Viard, M.
    KewalRamani, V. N.
    Wang, J. M.
    Blumenthal, R.
    Puri, A.

  2. Author Address

    Puri, A, NCI, Lab Expt & Computat Biol, Ctr Canc Res, NIH, POB B,Bldg 469,Room 211,Miller Dr, Frederick, MD 21702 USA NCI, Lab Expt & Computat Biol, Ctr Canc Res, NIH, Frederick, MD 21702 USA. NCI, HIV Drug Resistance Program, Canc Res Ctr, NIH, Frederick, MD 21701 USA. NIAID, Mol Microbiol Lab, NIH, Bethesda, MD 20892 USA. NCI, Mol Immunoregulat Lab, Canc Res Ctr, NIH, Frederick, MD 21701 USA.
    1. Year: 2004
  2. Journal: Virology
    1. 318
    2. 1
    3. Pages: 55-65
  4. Type of Article: Article
  1. Abstract:

    We had previously reported that glycosphingolipids (GSL) support human immunodeficiency virus type 1 (HIV-1) entry. In this study, we further examined this issue by expressing HIV-1 receptors in GSL-deficient GM95 cells. GM95 cells expressing low levels of CD4 and CXCR4 or CCR5 did not support HIV-1 Env-mediated fusion. However, higher expression of these receptors rendered GM95 cells highly susceptible to fusion with cells expressing appropriate HIV-1 envelope glycoproteins (HIV-1 Envs). The GM95 cells exhibited a different fusion phenotype when compared with GSL(+) NIH3T3 cells bearing similar receptor levels. Fusion of GM95 targets expressing higher levels of CD4 and coreceptors occurred at 25degreesC and was sensitive to cholesterol depletion or disruption of the cyloskeleton. In contrast, the fusion threshold of NIH3T3CD4X4/R5 targets was at greater than or equal to 28degreesC as previously reported and was insensitive to cholesterol depletion or cytoskeletal network disruption. On the basis of these observations, we propose that target membrane GSLs support HIV-1 Env-mediated fusion at low density of receptors by stabilizing receptor pools in natural targets. Published by Elsevier Inc

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