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

FEBS Letters

Garofalo, Tina²  Pavan, Antonio¹  Sorice, Maurizio²  Dolo, Vincenza¹  Longo, Agostina²  Gradini, Roberto²  Sale, Patrizio²  Mattei, Vincenzo²  Misasi, Roberta² 

[1] Dipartimento di Medicina Sperimentale, Università di L'Aquila, Via Vetoio Coppito 2, L'Aquila 67100, Italy;Dipartimento di Medicina Sperimentale e Patologia, Università di Roma ‘La Sapienza’, Viale Regina Elena 324, Rome 00161, Italy

关键词: GM3;    Ganglioside;    CXCR4;    gp120;    Microdomain;    PBL;    peripheral blood lymphocytes;    GEM;    glycosphingolipid-enriched microdomains;    PKC;    protein kinase C;    GPI;    glycosylphosphatidylinositol;    FCS;    fetal calf serum;    HPTLC;    high performance thin layer chromatography;    mAb;    monoclonal antibody;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;    PBS;    phosphate-buffered saline;    HRP;    horseradish peroxidase;    FITC;    fluorescein isothiocyanate;   

DOI  :  10.1016/S0014-5793(01)02830-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown