Evidence for cell surface association between CXCR4 and ganglioside GM3 after gp120 binding in SupT1 lymphoblastoid cells

FEBS Lett. 2001 Sep 28;506(1):55-60. doi: 10.1016/s0014-5793(01)02830-7.

Abstract

CXCR4 (fusin) is a chemokine receptor which is involved as a coreceptor in gp120 binding to the cell surface. In this study we provide evidence that binding of gp120 triggers CXCR4 recruitment to glycosphingolipid-enriched microdomains. Scanning confocal microscopy showed a nearly complete localization of CXCR4 within GM3-enriched plasma membrane domains of SupT1 cells and coimmunoprecipitation experiments revealed that CXCR4 was immunoprecipitated by IgG anti-GM3 after gp120 pretreatment. These findings reveal that gp120 binding induces a strict association between CXCR4 and ganglioside GM3, supporting the view that GM3 and CXCR4 are components of a functional multimolecular complex critical for HIV-1 entry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • Cell Membrane / metabolism
  • Chromatography, Thin Layer
  • G(M3) Ganglioside / metabolism*
  • HIV Envelope Protein gp120 / metabolism
  • Humans
  • Precipitin Tests
  • Protein Binding
  • Receptors, CXCR4 / metabolism*

Substances

  • G(M3) Ganglioside
  • HIV Envelope Protein gp120
  • Receptors, CXCR4