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Role of N ‐glycans and SDF‐1α on the coassociation of CD4 with CXCR4 at the plasma membrane of monocytic cells and blood lymphocytes
Author(s) -
Mbemba Elisabeth,
Saffar Line,
Gattegno Liliane
Publication year - 2002
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(02)02366-9
Subject(s) - cxcr4 , glycan , stromal cell , glycoprotein , human immunodeficiency virus (hiv) , biology , microbiology and biotechnology , immunology , chemistry , cancer research , chemokine , inflammation
CXCR4 is a coreceptor, along with CD4, for human immunodeficiency virus type 1 (HIV‐1). Trimolecular complexes between HIV‐1 glycoprotein (gp)120, CD4 and CXCR4 constitute a prerequisite for HIV entry. We studied whether CD4 is associated with CXCR4 on CD4+ CXCR4+ cells. Using the conformation‐dependent anti‐CXCR4 mAb 12G5, CD4 was coimmunoprecipitated with CXCR4 from the membrane of U937 cells which support HIV‐1 LAI efficient infection, and from that of peripheral blood lymphocytes (PBL). CD4 association with CXCR4 increased upon PBL coculture for 5 days with autologous monocytes, decreased upon treatment of the cells or the CD4‐CXCR4 complex with either N ‐glycanase or stromal cell derived factor‐1α (SDF‐1α) and was abolished by incubation of the cells with both, N ‐glycanase and SDF‐1α. This indicates that glycans are partly involved in CD4 association with CXCR4 and may partly explain the inhibitory effect of SDF‐1α on HIV infection.