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PMID: 11591370 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 506 ·No. 1 ·2001-09-28 ·Pages 55-60

Sorice M, Garofalo T, Misasi R, Longo A, Mattei V, Sale P, Dolo V, Gradini R, Pavan A

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.

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
Chemicals
G(M3) Ganglioside HIV Envelope Protein gp120 Receptors, CXCR4
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Sorice M
Dipartimento di Medicina Sperimentale e Patologia, Università de Roma La Sapienza, Italy.
Garofalo T
Misasi R
Longo A
Mattei V
Sale P
Dolo V
Gradini R
Pavan A
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2001-09-28
Pages
55-60
Language
English
Region
England
NLM ID
0155157
Subset
IM
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