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HTLV-1 uses HSPG and neuropilin-1 for entry by molecular mimicry of VEGF(165)

  1. Author:
    Lambert, S.
    Bouttier, M.
    Vassy, R.
    Seigneuret, M.
    Petrow-Sadowski, C.
    Janvier, S.
    Heveker, N.
    Ruscetti, F. W.
    Perret, G.
    Jones, K. S.
    Pique, C.

  2. Author Address

    Petrow-Sadowski, Cari, Jones, Kathryn S.] NCI, SAIC Frederick, Basic Sci Program, Frederick, MD 21702 USA. [Lambert, Sophie, Bouttier, Manuella, Seigneuret, Michel, Pique, Claudine] Univ Paris 05, CNRS, UMR 8104, Inserm U567, Paris, France. [Vassy, Roger, Perret, Gerrard] Univ Paris 13, UMR 7033, Bobigny, France. [Janvier, Sebastien, Heveker, Nikolaus] Univ Montreal, Hop St Justine, Ctr Rech 6737, Montreal, PQ H3T 1C5, Canada. [Janvier, Sebastien, Heveker, Nikolaus] Univ Montreal, Dept Biochim, Montreal, PQ H3C 3J7, Canada. [Ruscetti, Francis W.] NCI, Canc & Inflammat Program, Ctr Canc Res, Expt Immunol Lab, Frederick, MD 21702 USA.
    1. Year: 2009
  2. Journal: Blood
    1. 113
    2. 21
    3. Pages: 5176-5185
  4. Type of Article: Article
  1. Abstract:

    Human T-cell lymphotropic virus type 1 (HTLV-1) entry involves the interaction between the surface (SU) subunit of the Env proteins and cellular receptor(s). Previously, our laboratories demonstrated that heparan sulfate proteoglycans (HSPGs) and neuropilin-1 (NRP-1), a receptor of VEGF(165), are essential for HTLV-1 entry. Here we investigated whether, as when binding VEGF(165), HSPGs and NRP-1 work in concert during HTLV-1 entry. VEGF(165) binds to the b domain of NRP-1 through both HSPG-dependent and -independent interactions, the latter involving its exon 8. We show that VEGF(165) is a selective competitor of HTLV-1 entry and that HTLV-1 mimics VEGF(165) to recruit HSPGs and NRP-1: (1) the NRP-1 b domain is required for HTLV-1 binding, (2) SU binding to target cells is blocked by the HSPG-binding domain of VEGF(165); (3) the formation of Env/NRP-1 complexes is enhanced by HSPGs, and (4) the HTLV SU contains a motif homologous to VEGF(165) exon 8. This motif directly binds to NRP-1 and is essential for HTLV-1 binding to, internalization into, and infection of CD4(+) T cells and dendritic cells. These findings demonstrate that HSPGs and NRP-1 function as HTLV-1 receptors in a cooperative manner and reveal an unexpected mimicry mechanism that may have major implications in vivo. (Blood. 2009, 113: 5176-5185)

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  2. DOI: 10.1182/blood-2008-04-150342
  3. PMID: 19270265

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