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Evidence for cell surface association between CXCR4 and ganglioside GM3 after gp120 binding in SupT1 lymphoblastoid cells
Author(s) -
Sorice Maurizio,
Garofalo Tina,
Misasi Roberta,
Longo Agostina,
Mattei Vincenzo,
Sale Patrizio,
Dolo Vincenza,
Gradini Roberto,
Pavan Antonio
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02830-7
Subject(s) - cxcr4 , immunoprecipitation , ganglioside , microbiology and biotechnology , glycosphingolipid , chemokine receptor , confocal microscopy , confocal , receptor , biology , chemistry , chemokine , biophysics , biochemistry , immunology , antibody , geometry , mathematics
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.