Elisabeth Mbemba
University of Paris
22 Papers
218 Citations
Elisabeth Mbemba is an academic researcher from University of Paris. The author has contributed to research in topics: Tissue factor & Heparin. The author has an hindex of 12, co-authored 21 publications.
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Papers
A syndecan-4/CXCR4 complex expressed on human primary lymphocytes and macrophages and HeLa cell line binds the CXC chemokine stromal cell-derived factor-1 (SDF-1)
Morgan Hamon,Elisabeth Mbemba,Nathalie Charnaux,Hocine Slimani,Severine Brule,Line Saffar,Roger Vassy,Catherine Prost,N. Lièvre,Anna Starzec,Liliane Gattegno +10 more
TL;DR: It is shown that SDF-1 binds to high- and low-affinity sites on HeLa cells and that syndecan-4 from lymphocytes, monocyte derived-macrophages, and He La cells coimmunoprecipitated with CXCR4, the only known ligand of CX CR4, which is the coreceptor of X4 HIV strains.
Interaction of RANTES with syndecan-1 and syndecan-4 expressed by human primary macrophages.
Hocine Slimani,Nathalie Charnaux,Elisabeth Mbemba,Line Saffar,Roger Vassy,Claudio Vita,Liliane Gattegno +6 more
TL;DR: It is demonstrated that RANTES specifically binds to high and low affinity binding sites on human monocyte-derived macrophages (MDM), which suggests that glycosaminoglycans (GAGs) are involved in RantES binding to the PGs and that such bindings facilitate the subsequent interaction of RantingES with CCR5, on the MDM, characterized by low membrane expression of CCR 5.
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Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1α
TL;DR: The present data indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface.
Human alpha1-acid glycoprotein binds to CCR5 expressed on the plasma membrane of human primary macrophages.
TL;DR: The present study demonstrates that AGP binds specifically to MDM at high- and low-affinity binding sites with K(d) values of 16 nM and 4.9 microM respectively, and suggests that the inhibitory effect of AGP on the infection of human primary macrophages by R5 HIV-1 may be related to specific binding ofAGP to a macrophage membrane lectin or lectin-like component and to CCR5.
Molecular interaction between HIV-1 major envelope glycoprotein and dextran sulfate.
TL;DR: Results demonstrate the occurrence of a low affinity, but specific interaction between dextran sulfate and rgp160, which may account, at least in part, for the anti-HIV-1 activity of dextan sulfate.
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